Team:Michigan/Project
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== Hy-Bi: Virus Protein Surface Display == | == Hy-Bi: Virus Protein Surface Display == | ||
- | [[Image:vp130ex.jpg|530px|left|thumb| | + | [[Image:vp130ex.jpg|530px|left|thumb|Fig.5 The binding of the viral surface protein on algae cells: (A) algae without the virus surface proteins; (B) and (C) algae with virus surface proteins]] |
The idea is to express algae-binding proteins on the surface of E. Coli in order to cause flocculation. Flocculation is the aggregation and precipitation of particles from solution. This flocculation will make the formation of biodiesel more efficient by eliminating the need for centrifugation to concentrate the fuel source. | The idea is to express algae-binding proteins on the surface of E. Coli in order to cause flocculation. Flocculation is the aggregation and precipitation of particles from solution. This flocculation will make the formation of biodiesel more efficient by eliminating the need for centrifugation to concentrate the fuel source. | ||
- | We devised two ways to cause flocculation, one being using a pili expression and the other using a virus surface protein, and the subject of our group is the virus surface protein. During its viral attack on cells, virus needs a protein that enables it to attach to the surface of the host cells. One of the virus surface proteins, vp 130, is used by chlorovirus to attach itself onto the surface of algae. Onimatsu, et al. recombined the vp 130 gene from Chlorovirus CVK2 with a plasmid, producing a wealth of vp 130. The binding of these proteins on their host cells, chlorella, was detected using fluorescent vp 130 specific antibodies ( | + | We devised two ways to cause flocculation, one being using a pili expression and the other using a virus surface protein, and the subject of our group is the virus surface protein. During its viral attack on cells, virus needs a protein that enables it to attach to the surface of the host cells. One of the virus surface proteins, vp 130, is used by chlorovirus to attach itself onto the surface of algae. Onimatsu, et al. recombined the vp 130 gene from Chlorovirus CVK2 with a plasmid, producing a wealth of vp 130. The binding of these proteins on their host cells, chlorella, was detected using fluorescent vp 130 specific antibodies (Fig.5)[7]. |
- | [[Image:vp130.jpg|450px|left|thumb| | + | [[Image:vp130.jpg|450px|left|thumb|Fig.6 A model of vp 130-expressed bacteria binding algae cells.]] |
- | So, if we transfer the gene for this surface binding protein from the virus to E. Coli., each bacteria cell will bind to multiple algae cells, which bind to more bacteria, causing aggregation and flocculation. As opposed to using pili as the means to cause flocculation, the advantage of vp130 is its specific binding and aggregation of algae, automatically yielding a high algae mass in the flocculate ( | + | So, if we transfer the gene for this surface binding protein from the virus to E. Coli., each bacteria cell will bind to multiple algae cells, which bind to more bacteria, causing aggregation and flocculation. As opposed to using pili as the means to cause flocculation, the advantage of vp130 is its specific binding and aggregation of algae, automatically yielding a high algae mass in the flocculate (Fig.6). However, there are also disadvantages. For example, vp 130 is not a E. Coli surface protein, so it must be cloned as a fusion to a known surface protein. We also suspected OmpA and ice nucleation protein (INP) as candidate surface proteins. |
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Revision as of 22:45, 25 October 2010