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Virology. 2016 Apr;491:64-72. doi: 10.1016/j.virol.2016.01.010. Epub 2016 Feb 11.

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

Author information

1
State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
2
Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, China.
3
State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin 300071, China. Electronic address: liu2008@nankai.edu.cn.

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.

KEYWORDS:

Asparagine/Glutamine-rich layer; Conformational transition; Crystal structure; EIAV gp45; FPPR; HIV-1 gp41; Membrane fusion

PMID:
26874586
DOI:
10.1016/j.virol.2016.01.010
[Indexed for MEDLINE]
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