A human anti-HIV autoantibody enhances EBV transformation and HIV infection.


Journal Article

A highly specific, human IgG mAb, F223, which reacts with both HIV-1-infected cells and uninfected lymphoid cells, has been derived. F223 reacts with gp120 but fails to neutralize viral infection. The antibody does enhance HIV-1 infection in a complement-dependent manner. The autoantigen recognized by F223 is expressed on a small percentage of T cells and NK cells and the majority of B cells. Immunoprecipitation demonstrates F223 reactivity with an as of yet unidentified 159-kDa protein in uninfected lymphoid cells. This reactivity with uninfected cells is inhibited by free gp120 demonstrating the cross-reactive nature of this antibody. The F223 light chain demonstrates strong homology to VLlambda2 family genes whereas the heavy chain is most homologous (84%) to the germline gene VH3-H.11. In vivo usage of VH3 family genes by F223 and an anti-HIV-1 (gp41) human mAb, 3D6, with related autoreactivity, suggests that VH3 sequences may be important components of potentially pathogenic human anti-HIV-1 envelope autoantibodies. F223 was isolated from an HIV-1 infected individual with lymphoma and in vitro F223 significantly enhances EBV transformation of normal B cells and increases immunoglobulin production without affecting B cell proliferation. Characterization of this antibody response may provide important insights and mechanistic information on HIV pathogenesis.

Full Text

Duke Authors

Cited Authors

  • Cavacini, LA; Wisnewski, A; Peterson, JE; Montefiori, D; Emes, C; Duval, M; Kingsbury, G; Wang, A; Scadden, D; Posner, MR

Published Date

  • December 1999

Published In

Volume / Issue

  • 93 / 3

Start / End Page

  • 263 - 273

PubMed ID

  • 10600338

Pubmed Central ID

  • 10600338

International Standard Serial Number (ISSN)

  • 1521-6616

Digital Object Identifier (DOI)

  • 10.1006/clim.1999.4790


  • eng

Conference Location

  • United States