Abstract

The recent analysis of the first successful RV144 vaccine trial revealed that a high titer of plasma anti-V2 antibodies (Abs) correlated with a decreased risk of HIV-1 infection in vaccine recipients. To understand the mechanism of immune correlates, we studied seven anti-V2 monoclonal Abs (mAbs) developed from HIV-1 infected individuals. The V2 mAbs target conserved epitopes, including the binding site for α4β7 integrin, and are broadly cross-reactive with various gp120 proteins. Preferential usage of the VH1-69 gene by V2 mAbs may depend on selection by the same antigenic structure. Six of seven V2 mAbs weakly neutralized four to eight of the 41 pseudoviruses tested and resistance to neutralization was correlated with longer V2 domains. The data suggest the presence of shared, conserved structural elements in the V2 loop, and these can be used in the design of vaccine immunogens inducing broadly reactive Abs with anti-viral activities.

Links

Publisher Full Text

Authors

Gorny MK, Pan R, Williams C, Wang XH, Volsky B, O'Neal T, Spurrier B, Sampson JM, Li L, Seaman MS, Kong XP, Zolla-Pazner S

Institution

Department of Pathology, New York University School of Medicine, New York, NY 10016, USA. mirek.gorny@med.nyu.edu

Source

Virology 427:2 2012 Jun 5 pg 198-207

MeSH

AIDS Vaccines
Amino Acid Sequence
Antibodies, Monoclonal
Antibody Specificity
Antigens, Viral
Epitopes
HIV Antibodies
HIV Infections
HIV-1
Humans
Models, Molecular
Molecular Sequence Data
Protein Conformation

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22402248