Interactions of polyclonal and monoclonal anti-glycoprotein 120 antibodies with oligomeric glycoprotein 120-glycoprotein 41 complexes of a primary HIV type 1 isolate: relationship to neutralization.
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.
Fouts
T R
TR
Aaron Diamond AIDS Research Center, The Rockefeller University, New York, New York 10016, USA.
Trkola
A
A
Fung
M S
MS
Moore
J P
JP
D000911:Antibodies, Monoclonal / Q000276:immunology; D015483:HIV Antibodies / Q000276:immunology*; D015699:HIV Envelope Protein gp120 / Q000276:immunology*; D015700:HIV Envelope Protein gp41 / Q000276:immunology*; D015497:HIV-1 / Q000276:immunology*; D006801:Humans; D009500:Neutralization Tests; D009842:Oligopeptides / Q000276:immunology*
D000911:Antibodies, Monoclonal; D015483:HIV Antibodies; D015699:HIV Envelope Protein gp120; D015700:HIV Envelope Protein gp41; D009842:Oligopeptides