于湘晖
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- 姓名:于湘晖
- 目前身份:
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学术头衔:
博士生导师, 教育部“新世纪优秀人才支持计划”入选者
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学科领域:
生物化学
- 研究兴趣:
于湘晖,女,1972年7月22日出生, 汉族,博士,教授,现任吉林大学疫苗研究中心教授,博士生导师。
科研及获奖情况:作为项目负责人主持了1项国家自然科学基金、1项教育部“新世纪人才”资助计划和1项吉林省杰出青年资助计划,1项国家教育部留学回国人员资助计划,并参与多项国家“863”项目、自然科学基金项目和省部级项目。发表论文在SCI收录20篇,核心收录文章8篇,参与编写专著1本。被评为长春市优秀青年大学毕业生;吉林大学2006年优秀博士学位论文一等奖;2005至2006年度吉林大学“三八”红旗手。
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于湘晖, Bindong Liu, † Xianghui Yu, † Kun Luo, † Yunkai Yu, and Xiao-Fang Yu, *
JOURNAL OF VIROLOGY, Feb. 2004, p. 2072-2081,-0001,():
-1年11月30日
The Vif protein of human immunodeficiency virus type 1 (HIV-1) is essential for viral evasion of the host antiviral protein APOBEC3G, also known as CEM15. Vif mutant but not wild-type HIV-1 viruses produced in the presence of APOBEC3G have been shown to undergo hypermutations in newly synthesized viral DNA upon infection of target cells, presumably resulting from C-to-U modification during minus-strand viral DNA synthesis. We now report that HIV-1 Vif could induce rapid degradation of human APOBEC3G that was blocked by the proteasome inhibitor MG132. The efficiency of Vif-induced downregulation of APOBEC3G expression depended on the level of Vif expression. A single amino acid substitution in the conserved SLQXLA motif reduced Vif function. Vif proteins from distantly related primate lentiviruses such as SIVagm were unable to suppress the antiviral activity of human APOBEC3G or the packaging of APOBEC3G into HIV-1 Vif mutant virions, due to a lack of interaction with human APOBEC3G. In the presence of the proteasome inhibitor MG132, virion-associated Vif increased dramatically. However, increased virion packaging of Vif did not prevent virion packaging of APOBEC3G when proteasome function was impaired, and the infectivity of these virions was significantly reduced. These results suggest that Vif function is required during virus assembly to remove APOBEC3G from packaging into released virions. Once packaged, virion-associated Vif could not efficiently block the antiviral activity of APOBEC3G.
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于湘晖, Yunkai Yu, , Zuoxiang Xiao, Elana S. Ehrlich, Xianghui Yu, and Xiao-Fang Yu
GENES & DEVELOPMENT 18: 2867-2872,-0001,():
-1年11月30日
APOBEC3G, which induces hypermutations in newly synthesized viral DNA, is suppressed by HIV-1 Vif, acting through Cul5-ElonginB-ElonginC E3 ubiquitin ligase. We have now characterized a novel SOCS box in HIV-1 Vif that mediates its interaction with ElonginC. In this SOCS box, alanine replaces the consensus cysteine in the previously identified SOCS box. This new motif was necessary but insufficient for interaction with Cul5-ElonginB-ElonginC, as two highly conserved Cys residues outside the SOCS box were required to interact with Cul5 but not ElonginC. Therefore, selective assembly with Cul5 versus Cul2 E3 may require protein interfaces besides the SOCS-box-ElonginC interaction.
Cul5, APOBEC3G, E3 ubiquitin ligase, HIV-1 Vif, ElonginC, SOCS box
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于湘晖
,-0001,():
-1年11月30日
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