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Journal of Clinical Microbiology, Dec 1995, 3319-3323, Vol 33, No. 12
Copyright © 1995 by the American Society for Microbiology. All rights reserved.

Simple enzyme immunoassay for titration of antibodies to the CD4- binding site of human immunodeficiency virus type 1 gp120

I Turbica, M Posner, C Bruck and F Barin
Departement de Microbiologie Medicale et Moleculaire, Unite de Recherche Associee Centre National de la Recherche Scientifique 1334, Centre Hospitalier Universitaire Bretonneau, Tours, France.

We report the development of an immunoassay for the titration of antibody to the CD4-binding site (CD4BS) of the human immunodeficiency virus type 1 (HIV-1) surface glycoprotein gp120. This assay is a competitive enzyme-linked immunosorbent assay in which serum antibodies compete with labeled F105, a human monoclonal antibody whose corresponding epitope overlaps the conformation-dependent CD4BS, for binding to purified recombinant gp120 coated on a solid phase. Ninety- nine percent (109 of 110) of HIV-1-positive French patients and 91% (51 of 56) of HIV-1-positive African patients had CD4BS antibodies, indicating that the conformational CD4BS epitope is well conserved among different subtypes of HIV-1. Titers of CD4BS antibodies according to clinical status appeared to be not statistically different. A longitudinal study in 21 seroconverters showed that, for the majority of individuals, CD4BS antibodies appeared early and persisted at relatively high titers for several years. None of 21 HIV-2-seropositive patients had CD4BS antibodies in our assay, suggesting that the antibodies produced during HIV-2 infection are not cross-reactive with the CD4BS of HIV-1 gp120.

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