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Structural and functional characterization of EIAV gp45 fusion peptide proximal region and asparagine-rich layer

Abstract 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...

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Published in:Virology (New York, N.Y.) N.Y.), 2016-04, Vol.491, p.64-72
Main Authors: Duan, Liangwei, Du, Jiansen, Wang, Xuefeng, Zhou, Jianhua, Wang, Xiaojun, Liu, Xinqi
Format: Article
Language:English
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Summary:Abstract 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.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2016.01.010