Team:Cornell

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!align="center"|[[Team:Cornell/Notebook|Notebook]]
!align="center"|[[Team:Cornell/Notebook|Notebook]]
!align="center"|[[Team:Cornell/Team|The Team]]
!align="center"|[[Team:Cornell/Team|The Team]]
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!align="center"|[[Team:Cornell/Human Practices|Human Practices]]
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!align="center"|[[Team:Cornell/Outreach & Human Practices|Outreach & Human Practices]]
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!align="center"|[[Team:Cornell/Outreach|Outreach]]
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!align="center"|[[Team:Cornell/Safety|Safety]]
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!align="center"|[[Team:Cornell/Application|Application]]
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=Project Abstract=
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[[Image:CUTeam.JPG|right|500px]]
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=OMG OMVs!=
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[[Image:CUGEMZoo.jpg|right|500px]]
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Outer membrane vesicles (OMVs) are natural secretions by gram-negative bacteria that
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can transport various proteins, lipids, and nucleic acids in interactions with mammalian
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host cells. OMV technology presents an affordable, non-toxic, and direct method of drug
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delivery and antigen tracking. We have designed a method for visualizing the interactions
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of mammalian cells with outer membrane vesicles by utilizing the ClyA surface protein
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as an attachment site for fluorescent proteins. The current goal of this project is to
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characterize the distribution of varying ClyA-fluorescent protein complexes on OMVs.
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Future work will be to develop a tracking system employing two ClyA constructs:  a ClyA-fluorescent protein
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fusion for in vitro microscope imaging and a ClyA-single-chain antibody fragment to bind to an antigen.

Latest revision as of 20:57, 13 January 2011

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The Project Background Design Parts Submitted to the Registry Notebook The Team Outreach & Human Practices Safety Application


OMG OMVs!

CUGEMZoo.jpg

Outer membrane vesicles (OMVs) are natural secretions by gram-negative bacteria that can transport various proteins, lipids, and nucleic acids in interactions with mammalian host cells. OMV technology presents an affordable, non-toxic, and direct method of drug delivery and antigen tracking. We have designed a method for visualizing the interactions of mammalian cells with outer membrane vesicles by utilizing the ClyA surface protein as an attachment site for fluorescent proteins. The current goal of this project is to characterize the distribution of varying ClyA-fluorescent protein complexes on OMVs. Future work will be to develop a tracking system employing two ClyA constructs: a ClyA-fluorescent protein fusion for in vitro microscope imaging and a ClyA-single-chain antibody fragment to bind to an antigen.