Structural and functional characterization of EIAV gp45 fusion peptide proximal region and asparagine-rich layer
文献类型: 外文期刊
第一作者: Duan, Liangwei
作者: Duan, Liangwei;Du, Jiansen;Liu, Xinqi;Wang, Xuefeng;Zhou, Jianhua;Wang, Xiaojun
作者机构:
关键词: EIAV gp45;HIV-1 gp41;Crystal structure;FPPR;Asparagine/Glutamine-rich layer;Membrane fusion;Conformational transition
期刊名称:VIROLOGY ( 影响因子:3.616; 五年影响因子:3.967 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: Equine infectious anaemia virus (EIAV) and human immunodeficiency virus (HIV) are members of the lentiviral genus. Similar to HIV gp41, EIAV gp45 is a fusogenic protein that mediates fusion between the viral particle and the host cell membrane. The crystal structure of gp45 reported reveals a different conformation in the here that includes the fusion peptide proximal region (FPPR) and neighboring asparagine-rich layer compared with previous HIV-1 gp41 structures. A complicated hydrogen-bond network containing a cluster of solvent molecules appears to be critical for the stability of the gp45 helical bundle. Interestingly, viral replication was relatively unaffected by site-directed mutagenesis of EIAV, in striking contrast to that of HIV-1. Based on these observations, we speculate that EIAV is more adaptable to emergent mutations, which might be important for the evolution of EIAV as a quasi-species, and could potentially contribute to the success of the EIAV vaccine. (C) 2016 Elsevier Inc. All rights reserved.
分类号: R37
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