2015 Fiscal Year Final Research Report
Elucidation of SAMHD1-independent function of HIV/SIV Vpx
| Project/Area Number |
25460570
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Virology
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| Research Institution | Kumamoto University |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Keywords | HIV-2 / Vpx / SAMHD1 / 抗ウイルス宿主因子 / 変異体解析 / ポリプロリンモチーフ / 亜鉛フィンガー / マクロファージ |
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| Outline of Final Research Achievements |
HIV-2 Vpx has a function to degrade host anti-viral factor SAMHD1 in macrophages. We already showed SAMHD1 degradation-independent function in activated T cells, however the details remain elusive. This study was started to aim at elucidation of this function of Vpx. We first performed mutational analysis. As results, we found two mutants, C87A and P109A as candidates to have decreased SAMHD1 degradation-independent function, thus their details were examined. Finally, we got the following results: (1) C87 and the other three amino acids form zinc finger to stabilize protein. (2) poly-proline motif including P109 has various functions, e.g., to multimerize Vpx and regulate SAMHD1 degradation negatively, and to facilitate the specific degradation of SAMHD1 in macrophages. (3) There are no evidences that Vpx carries SAMHD1 degradation-independent function in macrophages. It can be considered that Vpx has this function in activated T cells, thus the detail is under the progress.
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| Free Research Field |
ウイルス学
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