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Functional and immunochemical cross-reactivity of V2-specific monoclonal antibodies from HIV-1-infected individuals.

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.

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  • 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