2011 Fiscal Year Final Research Report
Functional analysis of cellular membrane proteins for generation of viral envelope and transmission
| Project/Area Number |
21390137
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Virology
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Project Period (FY) |
2009 – 2011
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| Keywords | BST2 / HIV / エンベロープ / テザリン / 宿主因子 / BiFC / アクセサリー蛋白質 |
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| Research Abstract |
We performed a series of virological investigation of cellular membrane proteins on generation of HIV-1 envelope and release of HIV-1 particles. From functional examination of human BST2 that inhibits the release of HIV-1 particles from infected cells on release of viral particles, it was suggested that BST2 acts directly to HIV-1 because human BST2 has ability to inhibit HIV-1 from variety species of cells. Next, we found HIV-1 viral protein U(VPU), a specific antagonist of human BST2, that three amino acid(AA) residues(I34, L37, and L41) in the transmembrane(TM) domain of human BST2 are critical for the interaction with VPUand VPU-mediated antagonism of human BST2. Moreover, computer-assisted structural modeling suggests that an alignment of these four AA residues(I34, L37, L41, and T45) on the same helical face in the TM domain is crucial for the VPU-mediated antagonism of human BST2. These results contribute to the molecular understanding of human BST2 specific antagonism by HIV-1 VPU. On the other hand, we are unable to repeat to show contribution of TIP47 on incorporation of HIV-1 ENV in the viral particles.
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