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2024-03-28T18:13:19Z
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http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-28T01:05:41Z
<p>Nishantbpl: </p>
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<p align=center><embed src="https://static.igem.org/mediawiki/igem.org/5/51/Nish1.swf" width=900 height=500></p><br />
<br />
<p><h2>Special comments:</h2><br />
1.Plasmids acquired from Karolinska Institutet, Solna, Sweden. <br><br />
2.Safety page in 'Work' link.<br />
</div><br />
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</body><br />
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</html></div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-28T01:04:44Z
<p>Nishantbpl: </p>
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<p align=center><embed src="https://static.igem.org/mediawiki/igem.org/5/51/Nish1.swf" width=900 height=500></p><br />
<br />
<p><h2>Special comments:</h2><br><br />
1.Plasmids acquired from Karolinska Institutet, Solna, Sweden. <br><br />
2.Safety page in 'Work' link.<br />
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Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-28T00:56:47Z
<p>Nishantbpl: </p>
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Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-26T18:53:40Z
<p>Nishantbpl: </p>
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<br />
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<br />
<p align=center><embed src="https://static.igem.org/mediawiki/2010/5/51/Nish1.swf" width=900 height=500></p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
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style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
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<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
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<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-26T18:50:41Z
<p>Nishantbpl: </p>
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</head><br />
<br />
<body lang=EN-IN style='tab-interval:36.0pt'><br />
<br />
<div class=Section1><br />
<br />
<div style='mso-element:para-border-div;border:none;border-bottom:solid #4F81BD 1.0pt;<br />
mso-border-bottom-themecolor:accent1;padding:0cm 1cm 4.0pt 0cm'><br />
<embed src="https://static.igem.org/mediawiki/2010/5/51/Nish1.swf" width=900 height=500><br />
<p align=center>[[Image:IGEM_IITD_logo.png|200px]]</p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
<p class=MsoNormal><span style='mso-ansi-language:EN-IN;mso-fareast-language:<br />
EN-IN;mso-bidi-language:HI;mso-no-proof:yes'><!--[if gte vml 1]><v:shapetype<br />
id="_x0000_t75" coordsize="21600,21600" o:spt="75" o:preferrelative="t"<br />
path="m@4@5l@4@11@9@11@9@5xe" filled="f" stroked="f"><br />
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<v:imagedata src="IIT+Delhi+iGEM+Wiki_files/image001.png" o:title="Vector1"/><br />
</v:shape><![endif]--><![if !vml]><img width=260 height=279<br />
src="IIT+Delhi+iGEM+Wiki_files/image002.gif" alt=Vector1.png v:shapes="Picture_x0020_0"><![endif]></span><span<br />
lang=EN-US><span style='mso-spacerun:yes'> </span><span<br />
style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
EN-IN;mso-fareast-language:EN-IN;mso-bidi-language:HI;mso-no-proof:yes'><!--[if gte vml 1]><v:shape<br />
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style='width:195pt;height:212.25pt;visibility:visible;mso-wrap-style:square'><br />
<v:imagedata src="IIT+Delhi+iGEM+Wiki_files/image003.png" o:title="Vector2"/><br />
</v:shape><![endif]--><![if !vml]><img width=260 height=283<br />
src="IIT+Delhi+iGEM+Wiki_files/image004.gif" alt=Vector2.png v:shapes="Picture_x0020_1"><![endif]></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
</div><br />
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</body><br />
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</html><br />
<br />
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<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/File:Nish1.swf
File:Nish1.swf
2010-10-26T18:49:14Z
<p>Nishantbpl: uploaded a new version of "Image:Nish1.swf"</p>
<hr />
<div></div>
Nishantbpl
http://2010.igem.org/File:IITDweek1.txt
File:IITDweek1.txt
2010-10-18T06:46:42Z
<p>Nishantbpl: </p>
<hr />
<div></div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-18T06:45:56Z
<p>Nishantbpl: </p>
<hr />
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<br />
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<embed src="https://static.igem.org/mediawiki/2010/4/44/Nish2.swf" width=900 height=500><br />
<p align=center>[[Image:IGEM_IITD_logo.png|200px]]</p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
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style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
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<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
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<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-18T06:44:21Z
<p>Nishantbpl: </p>
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</head><br />
<br />
<body lang=EN-IN style='tab-interval:36.0pt'><br />
<br />
<div class=Section1><br />
<br />
<div style='mso-element:para-border-div;border:none;border-bottom:solid #4F81BD 1.0pt;<br />
mso-border-bottom-themecolor:accent1;padding:0cm 1cm 4.0pt 0cm'><br />
<embed src="https://static.igem.org/mediawiki/2010/5/51/Nish2.swf" width=900 height=500><br />
<p align=center>[[Image:IGEM_IITD_logo.png|200px]]</p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
<p class=MsoNormal><span style='mso-ansi-language:EN-IN;mso-fareast-language:<br />
EN-IN;mso-bidi-language:HI;mso-no-proof:yes'><!--[if gte vml 1]><v:shapetype<br />
id="_x0000_t75" coordsize="21600,21600" o:spt="75" o:preferrelative="t"<br />
path="m@4@5l@4@11@9@11@9@5xe" filled="f" stroked="f"><br />
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</v:shape><![endif]--><![if !vml]><img width=260 height=279<br />
src="IIT+Delhi+iGEM+Wiki_files/image002.gif" alt=Vector1.png v:shapes="Picture_x0020_0"><![endif]></span><span<br />
lang=EN-US><span style='mso-spacerun:yes'> </span><span<br />
style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
EN-IN;mso-fareast-language:EN-IN;mso-bidi-language:HI;mso-no-proof:yes'><!--[if gte vml 1]><v:shape<br />
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style='width:195pt;height:212.25pt;visibility:visible;mso-wrap-style:square'><br />
<v:imagedata src="IIT+Delhi+iGEM+Wiki_files/image003.png" o:title="Vector2"/><br />
</v:shape><![endif]--><![if !vml]><img width=260 height=283<br />
src="IIT+Delhi+iGEM+Wiki_files/image004.gif" alt=Vector2.png v:shapes="Picture_x0020_1"><![endif]></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
</div><br />
<br />
</body><br />
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</html><br />
<br />
<br />
<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/File:Nish2.swf
File:Nish2.swf
2010-10-18T06:43:39Z
<p>Nishantbpl: </p>
<hr />
<div></div>
Nishantbpl
http://2010.igem.org/File:Nish1.swf
File:Nish1.swf
2010-10-18T06:39:00Z
<p>Nishantbpl: uploaded a new version of "Image:Nish1.swf"</p>
<hr />
<div></div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-18T03:37:47Z
<p>Nishantbpl: </p>
<hr />
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<br />
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<embed src="https://static.igem.org/mediawiki/2010/5/51/Nish1.swf" width=900 height=500><br />
<p align=center>[[Image:IGEM_IITD_logo.png|200px]]</p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
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style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
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<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
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<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-18T03:36:21Z
<p>Nishantbpl: </p>
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</head><br />
<br />
<body lang=EN-IN style='tab-interval:36.0pt'><br />
<br />
<div class=Section1><br />
<br />
<div style='mso-element:para-border-div;border:none;border-bottom:solid #4F81BD 1.0pt;<br />
mso-border-bottom-themecolor:accent1;padding:0cm 1cm 4.0pt 0cm'><br />
<p align=center>[[Image:IGEM_IITD_logo.png|200px]]</p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
<p class=MsoNormal><span style='mso-ansi-language:EN-IN;mso-fareast-language:<br />
EN-IN;mso-bidi-language:HI;mso-no-proof:yes'><!--[if gte vml 1]><v:shapetype<br />
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</v:shape><![endif]--><![if !vml]><img width=260 height=279<br />
src="IIT+Delhi+iGEM+Wiki_files/image002.gif" alt=Vector1.png v:shapes="Picture_x0020_0"><![endif]></span><span<br />
lang=EN-US><span style='mso-spacerun:yes'> </span><span<br />
style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
EN-IN;mso-fareast-language:EN-IN;mso-bidi-language:HI;mso-no-proof:yes'><!--[if gte vml 1]><v:shape<br />
id="Picture_x0020_1" o:spid="_x0000_i1025" type="#_x0000_t75" alt="Vector2.png"<br />
style='width:195pt;height:212.25pt;visibility:visible;mso-wrap-style:square'><br />
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src="IIT+Delhi+iGEM+Wiki_files/image004.gif" alt=Vector2.png v:shapes="Picture_x0020_1"><![endif]></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
</div><br />
<br />
</body><br />
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</html><br />
<br />
<br />
<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-18T03:35:46Z
<p>Nishantbpl: </p>
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<div class=Section1><br />
<br />
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mso-border-bottom-themecolor:accent1;padding:0cm 1cm 4.0pt 0cm'><br />
<p align=center>[[Image:IGEM_IITD_logo.png|200px]]</p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
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style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
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<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
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<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-18T03:20:38Z
<p>Nishantbpl: </p>
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</head><br />
<br />
<body lang=EN-IN style='tab-interval:36.0pt'><br />
<br />
<div class=Section1><br />
<br />
<div style='mso-element:para-border-div;border:none;border-bottom:solid #4F81BD 1.0pt;<br />
mso-border-bottom-themecolor:accent1;padding:0cm 1cm 4.0pt 0cm'><br />
<embedhttps://static.igem.org/mediawiki/2010/5/51/Nish1.swf<br />
<p align=center>[[Image:IGEM_IITD_logo.png|200px]]</p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
<p class=MsoNormal><span style='mso-ansi-language:EN-IN;mso-fareast-language:<br />
EN-IN;mso-bidi-language:HI;mso-no-proof:yes'><!--[if gte vml 1]><v:shapetype<br />
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</v:shape><![endif]--><![if !vml]><img width=260 height=279<br />
src="IIT+Delhi+iGEM+Wiki_files/image002.gif" alt=Vector1.png v:shapes="Picture_x0020_0"><![endif]></span><span<br />
lang=EN-US><span style='mso-spacerun:yes'> </span><span<br />
style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
EN-IN;mso-fareast-language:EN-IN;mso-bidi-language:HI;mso-no-proof:yes'><!--[if gte vml 1]><v:shape<br />
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style='width:195pt;height:212.25pt;visibility:visible;mso-wrap-style:square'><br />
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src="IIT+Delhi+iGEM+Wiki_files/image004.gif" alt=Vector2.png v:shapes="Picture_x0020_1"><![endif]></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
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</body><br />
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</html><br />
<br />
<br />
<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-18T03:02:00Z
<p>Nishantbpl: </p>
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<br />
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<br />
<p align=center><img src="https://static.igem.org/mediawiki/2010/5/58/IGEM_IITD_logo.png" width="100"/></p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b><o:p></o:p></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
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style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
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<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
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''Italic text''</div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-17T19:00:52Z
<p>Nishantbpl: </p>
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</head><br />
<br />
<body lang=EN-IN style='tab-interval:36.0pt'><br />
<br />
<div class=Section1><br />
<br />
<div style='mso-element:para-border-div;border:none;border-bottom:solid #4F81BD 1.0pt;<br />
mso-border-bottom-themecolor:accent1;padding:0cm 1cm 4.0pt 0cm'><br />
<br />
<embed src="https://static.igem.org/mediawiki/2010/5/51/Nish1.swf" width=900 height=500><br />
<br />
<p align=center><img src="https://static.igem.org/mediawiki/2010/5/58/IGEM_IITD_logo.png" width="100"/></p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b><o:p></o:p></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
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lang=EN-US><span style='mso-spacerun:yes'> </span><span<br />
style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
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<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
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<br />
{| style="color:#1b2c8a;background-color:#0c6;" cellpadding="3" cellspacing="1" border="1" bordercolor="#fff" width="62%" align="center"<br />
!align="center"|[[Team:IIT_Delhi_1|Home]]<br />
!align="center"|[[Team:IIT_Delhi_1/Team|Team]]<br />
!align="center"|[https://igem.org/Team.cgi?year=2010&team_name=IIT_Delhi_1 Official Team Profile]<br />
!align="center"|[[Team:IIT_Delhi_1/Project|Project]]<br />
!align="center"|[[Team:IIT_Delhi_1/Parts|Parts Submitted to the Registry]]<br />
!align="center"|[[Team:IIT_Delhi_1/Modeling|Modeling]]<br />
!align="center"|[[Team:IIT_Delhi_1/Notebook|Notebook]]<br />
!align="center"|[[Team:IIT_Delhi_1/Safety|Safety]]<br />
|}<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-17T18:57:50Z
<p>Nishantbpl: </p>
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<br />
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<br />
<a href="https://static.igem.org/mediawiki/2010/5/51/Nish1.swf">Flash Version</a><br />
<br />
<p align=center><img src="https://static.igem.org/mediawiki/2010/5/58/IGEM_IITD_logo.png" width="100"/></p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b><o:p></o:p></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
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lang=EN-US><span style='mso-spacerun:yes'> </span><span<br />
style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
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<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
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<br />
<br />
{| style="color:#1b2c8a;background-color:#0c6;" cellpadding="3" cellspacing="1" border="1" bordercolor="#fff" width="62%" align="center"<br />
!align="center"|[[Team:IIT_Delhi_1|Home]]<br />
!align="center"|[[Team:IIT_Delhi_1/Team|Team]]<br />
!align="center"|[https://igem.org/Team.cgi?year=2010&team_name=IIT_Delhi_1 Official Team Profile]<br />
!align="center"|[[Team:IIT_Delhi_1/Project|Project]]<br />
!align="center"|[[Team:IIT_Delhi_1/Parts|Parts Submitted to the Registry]]<br />
!align="center"|[[Team:IIT_Delhi_1/Modeling|Modeling]]<br />
!align="center"|[[Team:IIT_Delhi_1/Notebook|Notebook]]<br />
!align="center"|[[Team:IIT_Delhi_1/Safety|Safety]]<br />
|}<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/File:Nish1.swf
File:Nish1.swf
2010-10-16T19:14:34Z
<p>Nishantbpl: uploaded a new version of "Image:Nish1.swf": Reverted to version as of 18:32, 16 October 2010</p>
<hr />
<div></div>
Nishantbpl
http://2010.igem.org/File:Nish1.swf
File:Nish1.swf
2010-10-16T19:13:14Z
<p>Nishantbpl: uploaded a new version of "Image:Nish1.swf"</p>
<hr />
<div></div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-16T19:12:46Z
<p>Nishantbpl: </p>
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</head><br />
<br />
<body lang=EN-IN style='tab-interval:36.0pt'><br />
<br />
<div class=Section1><br />
<br />
<div style='mso-element:para-border-div;border:none;border-bottom:solid #4F81BD 1.0pt;<br />
mso-border-bottom-themecolor:accent1;padding:0cm 1cm 4.0pt 0cm'><br />
<br />
[[Image:IGEM_IITD_logo.png]]<br />
<br />
<p align=center><img src="https://static.igem.org/mediawiki/2010/5/58/IGEM_IITD_logo.png" width="100"/></p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'><b>Dr. Coli </b><o:p></o:p></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h2><span lang=EN-US><u>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
<p class=MsoNormal><span style='mso-ansi-language:EN-IN;mso-fareast-language:<br />
EN-IN;mso-bidi-language:HI;mso-no-proof:yes'><!--[if gte vml 1]><v:shapetype<br />
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src="IIT+Delhi+iGEM+Wiki_files/image002.gif" alt=Vector1.png v:shapes="Picture_x0020_0"><![endif]></span><span<br />
lang=EN-US><span style='mso-spacerun:yes'> </span><span<br />
style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
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src="IIT+Delhi+iGEM+Wiki_files/image004.gif" alt=Vector2.png v:shapes="Picture_x0020_1"><![endif]></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
</div><br />
<br />
</body><br />
<br />
</html><br />
<br />
<br />
{| style="color:#1b2c8a;background-color:#0c6;" cellpadding="3" cellspacing="1" border="1" bordercolor="#fff" width="62%" align="center"<br />
!align="center"|[[Team:IIT_Delhi_1|Home]]<br />
!align="center"|[[Team:IIT_Delhi_1/Team|Team]]<br />
!align="center"|[https://igem.org/Team.cgi?year=2010&team_name=IIT_Delhi_1 Official Team Profile]<br />
!align="center"|[[Team:IIT_Delhi_1/Project|Project]]<br />
!align="center"|[[Team:IIT_Delhi_1/Parts|Parts Submitted to the Registry]]<br />
!align="center"|[[Team:IIT_Delhi_1/Modeling|Modeling]]<br />
!align="center"|[[Team:IIT_Delhi_1/Notebook|Notebook]]<br />
!align="center"|[[Team:IIT_Delhi_1/Safety|Safety]]<br />
|}<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/File:Nish1.swf
File:Nish1.swf
2010-10-16T18:32:46Z
<p>Nishantbpl: </p>
<hr />
<div></div>
Nishantbpl
http://2010.igem.org/User:Nishantbpl
User:Nishantbpl
2010-10-16T18:29:10Z
<p>Nishantbpl: New page: Hi, I am Nishant Shrivastava from IIT delhi.</p>
<hr />
<div>Hi, I am Nishant Shrivastava from IIT delhi.</div>
Nishantbpl
http://2010.igem.org/Team:IIT_Delhi_1
Team:IIT Delhi 1
2010-10-16T07:44:47Z
<p>Nishantbpl: </p>
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<br />
<div class=Section1><br />
<br />
<div style='mso-element:para-border-div;border:none;border-bottom:solid #4F81BD 1.0pt;<br />
mso-border-bottom-themecolor:accent1;padding:0cm 0cm 4.0pt 0cm'><br />
<br />
<p align=center><img src="https://static.igem.org/mediawiki/2010/5/58/IGEM_IITD_logo.png" width="300"/></p><br />
<br />
<p class=MsoTitle align=center style='text-align:center'><span lang=EN-US><i style='mso-bidi-font-style:<br />
normal'>Dr. Coli <o:p></o:p></i></span></p><br />
<br />
</div><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h2><u><span lang=EN-US>Renin Angiotensin Aldosterone System (RAAS)<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The Renin<br />
Angiotensin Aldosterone System is a hormone system in the human body that is<br />
responsible for the regulation of blood pressure and fluid balance.</span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>A decrease in<br />
renal perfusion causes the release of the enzyme renin which subsequently<br />
cleaves angiotensinogen to angiotensin I. This is further converted to<br />
angiotensin II by angiotensin-converting enzyme (ACE). The bioactive product,<br />
angiotensin II, causes the constriction of blood vessels, leading to an<br />
increased blood pressure. It is also responsible for the secretion of<br />
aldosterone by the adrenal cortex, which acts by increasing the re-absorption<br />
of sodium and water into the blood. Hence, the fluid volume as well as the<br />
blood pressure is maintained in the body.</span></p><br />
<br />
<h2><u><span lang=EN-US>The &#945;-hemolysin System in <i style='mso-bidi-font-style:<br />
normal'>E.coli<o:p></o:p></i></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The<br />
alpha-hemolysin system is a type I secretion system found in wild type <i<br />
style='mso-bidi-font-style:normal'>E.coli </i>which enable them to cause<br />
infection in the urinary tract and is an important virulence factor because of<br />
its cytotoxic and cytolytic activity against a variety of mammalian cells. </span></p><br />
<br />
<h3 style='text-align:justify'><span lang=EN-US>Functioning</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The hemolysin<br />
system originates from a series of hly genes. These genes are present in the<br />
series <i style='mso-bidi-font-style:normal'>hlyC – hlyA – hlyB – hlyD</i>. Of<br />
these, <i style='mso-bidi-font-style:normal'>hlyA</i> codes for the protein<br />
that is responsible for the infection. Hly B and D are membrane proteins that<br />
work in coordination for the secretion of HlyA. The synthesis, activation and<br />
secretion of HlyA in <i style='mso-bidi-font-style:normal'>E.coli </i>is<br />
determined by the <i style='mso-bidi-font-style:normal'>hlyCABD</i> operon. This<br />
operon is either located either on the chromosome or on transmissible plasmids.<br />
<br />
</span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>It has been<br />
shown that this system can be used to produce and secrete a protein of our<br />
choice if the protein contains 60 amino acid residues from the carboxy terminal<br />
end of the HlyA protein. </span></p><br />
<br />
<h2><u><span lang=EN-US>Our iGEM 2010 Project<o:p></o:p></span></u></h2><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<h3><span lang=EN-US>Introduction</span></h3><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>Our aim is to<br />
create an online elicitor detection and response in a flow system, which can<br />
function in the detection of high blood pressure and help reduce it by<br />
releasing renin inhibitors into the circulatory system. This kind of a system<br />
would be helpful to patients with a hypertensive condition. </span></p><br />
<br />
<h3><span lang=EN-US>Approach</span></h3><br />
<br />
<p class=MsoNormal><span lang=EN-US>Since the blood pressure system is not<br />
really a chemical signal, what we have assumed is that the blood pressure can<br />
be easily converted into a chemical signal. Having assumed this, we will use a<br />
chemical signal such as IPTG or AHL as the elicitor to produce appropriate<br />
amounts of renin inhibitor. For easy detection and verification, we are<br />
planning to use GFP in place of renin inhibitor which can easily be replaced<br />
later.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>For this we will be introducing two vectors<br />
into <i style='mso-bidi-font-style:normal'>E. coli </i>as shown below.</span></p><br />
<br />
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style='mso-tab-count:1'> </span></span><span style='mso-ansi-language:<br />
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<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US>The first vector<br />
which contains the GFP-hlyA chimeric sequence with pLac promoter is used to<br />
produce the chimera GFP protein which contains 62 amino acid residues from the<br />
C terminal of hlyA protein, a prerequisite for the secretion of the protein<br />
outside the cell body. Forming a chimera will not in any way change the<br />
structure or function as per literature.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>The other vector contains the hlyB and hlyD<br />
sequences with ptet promoter sequence. These two proteins will be<br />
constitutively expressed. These proteins are present in the membrane and<br />
provide for an outlet of hlyA or chimeras with 62 amino acid residues of the C<br />
terminal of hlyA.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>After we are successful in obtaining<br />
GFP-hlyA chimera outside the cell body, our next task will be to immobilize<br />
these cells in a flow system and characterize the flow-expression profile. We<br />
would want to keep the cells in G0 phase so as to have continuous expression of<br />
the protein without cell death</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US>We will also be working towards minimizing<br />
the toxins and other products so that such a system can finally be thought fit<br />
for incorporating and integrating with the circulatory system in our body.</span></p><br />
<br />
<p class=MsoNormal><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
<p class=MsoNormal style='text-align:justify'><span lang=EN-US><o:p>&nbsp;</o:p></span></p><br />
<br />
</div><br />
<br />
</body><br />
<br />
</html><br />
<br />
<br />
{| style="color:#1b2c8a;background-color:#0c6;" cellpadding="3" cellspacing="1" border="1" bordercolor="#fff" width="62%" align="center"<br />
!align="center"|[[Team:IIT_Delhi_1|Home]]<br />
!align="center"|[[Team:IIT_Delhi_1/Team|Team]]<br />
!align="center"|[https://igem.org/Team.cgi?year=2010&team_name=IIT_Delhi_1 Official Team Profile]<br />
!align="center"|[[Team:IIT_Delhi_1/Project|Project]]<br />
!align="center"|[[Team:IIT_Delhi_1/Parts|Parts Submitted to the Registry]]<br />
!align="center"|[[Team:IIT_Delhi_1/Modeling|Modeling]]<br />
!align="center"|[[Team:IIT_Delhi_1/Notebook|Notebook]]<br />
!align="center"|[[Team:IIT_Delhi_1/Safety|Safety]]<br />
|}<br />
''Italic text''</div>
Nishantbpl
http://2010.igem.org/File:IGEM_IITD_logo.png
File:IGEM IITD logo.png
2010-10-16T07:40:53Z
<p>Nishantbpl: IITD Team logo</p>
<hr />
<div>IITD Team logo</div>
Nishantbpl
http://2010.igem.org/File:IIT_Delhi_1_logo.png
File:IIT Delhi 1 logo.png
2010-04-23T11:53:08Z
<p>Nishantbpl: Indian Institute of Technology Delhi</p>
<hr />
<div>Indian Institute of Technology Delhi</div>
Nishantbpl