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.

doi:10.1128/JVI.69.10.6191-6198.1995

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Article

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.

Journal of virology - 1 Oct 1995

Stamatatos L, Cheng-Mayer C

Abstract excerpt

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...

Topics

Amino Acid Sequence
Animals
Antibodies, Monoclonal
Antigen-Antibody Complex
Binding Sites, Antibody
CD4 Antigens
Epitopes
Genetic Variation
HIV Envelope Protein gp120
HIV-1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Humans

Kinetics

Mice

Molecular Sequence Data

Protein Conformation

Virion

Source

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Identifiers

PMID: 7545244
DOI: 10.1128/JVI.69.10.6191-6198.1995
PMCID: PMC189516

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7545244-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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