Document 1150 DOCN M9591150 TI Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. DT 9509 AU Sattentau QJ; Moore JP; Centre d'Immunologie de Marseille Luminy, Marseille, France. SO J Exp Med. 1995 Jul 1;182(1):185-96. Unique Identifier : AIDSLINE MED/95310850 AB The major target of the neutralizing antibody response to infection by the human immunodeficiency virus type 1 (HIV-1) is the outer envelope glycoprotein, gp120. The spectrum of HIV-1 neutralization specificity is currently represented by monoclonal antibodies (mAbs) that can be divided broadly into five groups. We have studied the binding of these mAbs to functional oligomeric and soluble monomeric gp120 derived from the molecular clone of a cell line-adapted isolate of HIV-1, and compared these binding properties with virus neutralization. Binding of all mAbs except those reactive with the V3 loop was much weaker to oligomeric than to monomeric gp120. This reduction in binding to oligomeric gp120 was determined mostly by a slower relative rate of association, although the dissociation rate also had some influence on relative variation in mAb affinity. Virus neutralization correlated broadly with mAb binding to the oligomeric rather than to the monomeric form of gp120, and neutralization potency was related to the estimated association rate. Thus, with the exception of the hypervariable V3 loop, regions of HIV-1 gp120 with the potential to induce a neutralization response are likely to be poorly presented for antibody recognition on the surface of cell line-adapted virions. DE Antibodies, Monoclonal/*IMMUNOLOGY/METABOLISM Antibody Affinity Antigen-Antibody Reactions Antigenic Determinants/*IMMUNOLOGY/METABOLISM Antigens, CD4/METABOLISM Cell Line Comparative Study Human HIV Antibodies/*IMMUNOLOGY/METABOLISM HIV Envelope Protein gp120/*IMMUNOLOGY/METABOLISM HIV-1/*IMMUNOLOGY Neutralization Tests Peptide Fragments/IMMUNOLOGY/METABOLISM Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. Virion/IMMUNOLOGY JOURNAL ARTICLE SOURCE: National Library of Medicine. NOTICE: This material may be protected by Copyright Law (Title 17, U.S.Code).