| Literature DB >> 9591713 |
T R Fouts1, A Trkola, M S Fung, J P Moore.
Abstract
We have studied antibody reactivity with monomeric and oligomeric forms of the gp120 envelope glycoprotein from the macrophage-tropic primary virus, HIV-1 JR-FL. We find that the correlation between oligomer reactivity and virus neutralization is not absolute for MAbs to epitopes overlapping the CD4-binding site on gp120. An MAb (205-46-9) with very limited neutralizing ability for JR-FL binds about as avidly to oligomeric JR-FL envelope glycoproteins as the strongly neutralizing IgG1b12 MAb does. In addition, neutralizing and nonneutralizing sera from HIV-1-infected people are similar in their reactivities to oligomeric JR-FL envelope glycoproteins; the correlation between oligomer reactivity and virus neutralization is weak. Although oligomer reactivity of an anti-gp120 antibody is necessary for virus neutralization, it is not always sufficient to cause it.Entities:
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Year: 1998 PMID: 9591713 DOI: 10.1089/aid.1998.14.591
Source DB: PubMed Journal: AIDS Res Hum Retroviruses ISSN: 0889-2229 Impact factor: 2.205