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J. Virol., Oct 1995, 6191-6198, Vol 69, No. 10
L Stamatatos and C Cheng-Mayer
We investigated the binding of conformation-dependent anti-V2, anti-V3, and
anti-CD4-binding site monoclonal antibodies to monomeric and virion-
associated gp120 from human immunodeficiency virus type 1 isolates
displaying marked differences in cell tropism. For all viruses examined, we
found that the half-maximal binding values of the anti-V2 and
anti-CD4-binding site antibodies with virion-associated gp120 were higher
than those with monomeric gp120, but the maximum amount of antibodies bound
was diminished only for one of the anti-V2 antibodies tested. These
observations suggest that upon gp120 oligomerization, the V2 loop and
CD4-binding site undergo conformational changes and that particular
epitopes within these domains are occluded in the oligomeric gp120. In
contrast, although the overall binding patterns and half- maximal binding
values of the anti-V3 loop antibodies tested were similar with monomeric
and oligomeric gp120, all the V3 loop epitopes examined were less
accessible to antibody binding on the virion surface. This masking of the
V3 loop is more pronounced for the primary- like macrophage-tropic isolates
examined. Lastly, we observe that upon soluble receptor-virion binding,
specific V3 loop epitopes that differ for viruses displaying different
tropisms are exposed.
Copyright © 1995, American Society for Microbiology
Structural modulations of the envelope gp120 glycoprotein of human immunodeficiency virus type 1 upon oligomerization and differential V3 loop epitope exposure of isolates displaying distinct tropism upon virion-soluble receptor binding
Aaron Diamond AIDS Research Center, New York University School of Medicine, New York 10016, USA.
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