The HIV-1 gp120 V1V2 loop: Structure, function and importance for vaccine development

Robert J. O'Connell*, Jerome H. Kim, Jean Louis Excler

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

25 Scopus citations

Abstract

Although the second variable loop (V2) of the HIV-1 gp120 envelope glycoprotein shows substantial sequence diversity between strains, its functional importance imposes critical conservation of structure, and within particular microdomains, of sequence. V2 influences HIV-1 viral entry by contributing to trimer stabilization and co-receptor binding. It is one of 4 key domains targeted by the broadly neutralizing antibodies that arise during HIV-1 infection. HIV-1 uses V1V2 sequence variation and glycosylation to escape neutralizing antibody. In the Thai Phase III HIV-1 vaccine trial, RV144, vaccine-induced IgG against V1V2 inversely correlated with the risk of HIV-1 acquisition, and HIV-1 strains infecting RV144 vaccine recipients differed from those infecting placebo recipients in the V2 domain. Similarly, non-human primate challenge studies demonstrated an inverse correlation between vaccine-induced anti-V2 responses and simian immunodeficiency virus acquisition. We hypothesize that increased magnitude, frequency and duration of vaccine-induced anti-V2 antibody responses should improve efficacy afforded by pox-protein prime-boost HIV vaccine strategies.

Original languageEnglish
Pages (from-to)1489-1500
Number of pages12
JournalExpert Review of Vaccines
Volume13
Issue number12
DOIs
StatePublished - 1 Dec 2014
Externally publishedYes

Keywords

  • Efficacy
  • HIV vaccine
  • Neutralizing antibodies
  • Nonneutralizing antibodies
  • RV144
  • V1V2 loop
  • gp120

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