Contribution of the gp120 V3 loop to envelope glycoprotein trimer stability in primate immunodeficiency viruses.

Abstract:

:The V3 loop of the human immunodeficiency virus type 1 (HIV-1) gp120 exterior envelope glycoprotein (Env) becomes exposed after CD4 binding and contacts the coreceptor to mediate viral entry. Prior to CD4 engagement, a hydrophobic patch located at the tip of the V3 loop stabilizes the non-covalent association of gp120 with the Env trimer of HIV-1 subtype B strains. Here, we show that this conserved hydrophobic patch (amino acid residues 307, 309 and 317) contributes to gp120-trimer association in HIV-1 subtype C, HIV-2 and SIV. Changes that reduced the hydrophobicity of these V3 residues resulted in increased gp120 shedding and decreased Env-mediated cell-cell fusion and virus entry in the different primate immunodeficiency viruses tested. Thus, the hydrophobic patch is an evolutionarily conserved element in the tip of the gp120 V3 loop that plays an essential role in maintaining the stability of the pre-triggered Env trimer in diverse primate immunodeficiency viruses.

journal_name

Virology

journal_title

Virology

authors

Bowder D,Hollingsead H,Durst K,Hu D,Wei W,Wiggins J,Medjahed H,Finzi A,Sodroski J,Xiang SH

doi

10.1016/j.virol.2018.06.005

subject

Has Abstract

pub_date

2018-08-01 00:00:00

pages

158-168

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(18)30182-X

journal_volume

521

pub_type

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