The HIV-1 gp120 V1V2 loop: structure, function and importance for vaccine development. (December 2014)

• Record Type: Journal Article
• Authors: O'Connell, Robert J; Kim, Jerome H; Excler, Jean-Louis
• Is Part Of: Expert review of vaccines. Volume 13:Number 12(2014)
• Page Start: 1489
• Page End: 1500
• Publication Date: 2014-12
• Subjects: Vaccines -- Periodicals; Vaccination -- Periodicals; 615.37205
• DOI: 10.1586/14760584.2014.951335
• Languages: English
• ISSNs: 1476-0584

Abstract

<abstract> <title> <x xml:space="preserve">Abstract</x> </title> <p>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.</p> </abstract>