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

Dane Bowder, Haley Hollingsead, Kate Durst, Duoyi Hu, Wenzhong Wei, Joshua Wiggins, Halima Medjahed, Andrés Finzi, Joseph Sodroski, Shi Hua Xiang

Research output: Contribution to journalArticle

1 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)158-168
Number of pages11
JournalVirology
Volume521
DOIs
StatePublished - Aug 2018

Keywords

  • HIV-1
  • HIV-2
  • Hydrophobic patch
  • Primate immunodeficiency viruses (PIV)
  • Simian immunodeficiency virus (SIV)
  • V3 loop
  • gp120

ASJC Scopus subject areas

  • Virology

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  • Cite this

    Bowder, D., Hollingsead, H., Durst, K., Hu, D., Wei, W., Wiggins, J., Medjahed, H., Finzi, A., Sodroski, J., & Xiang, S. H. (2018). Contribution of the gp120 V3 loop to envelope glycoprotein trimer stability in primate immunodeficiency viruses. Virology, 521, 158-168. https://doi.org/10.1016/j.virol.2018.06.005