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The role of the third variable domain (V3) of gp120 in the neutralization of primary and T-cell line adapted (TCLA) strains of human immunodeficiency virus type 1 (HIV-1) by serum from HIV-1-infected individuals was investigated. A primary virus isolate, M2424/4, when adapted to H9 cells, was more sensitive to neutralization on MT2 cells than the same stock passaged in PBMC. Neutralization of the PBMC-passaged stock by V3-specific MAbs was abrogated by addition of V3 (MN) peptide. However, exogenous V3 (MN) peptide failed to reduce the neutralization of this isolate on PBMC, or MT2 cells, by high titre anti-HIV-1 polyclonal human sera in contrast to the extensive reduction of neutralization by the same sera on MT2 cells using the prototype MN strain (4- to > or = 24-fold) and the TCLA M2424/H9 isolate (2- to 8-fold). These results indicate that the neutralization of primary virus isolates by serum from HIV-1-infected individuals is not significantly mediated by V3-specific antibodies.

Original publication

DOI

10.1099/0022-1317-79-1-77

Type

Journal article

Journal

J Gen Virol

Publication Date

01/1998

Volume

79 ( Pt 1)

Pages

77 - 82

Keywords

Adaptation, Biological, Amino Acid Sequence, Base Sequence, Cells, Cultured, DNA, Viral, HIV Antibodies, HIV Antigens, HIV Core Protein p24, HIV Envelope Protein gp120, HIV-1, Humans, Molecular Sequence Data, Neutralization Tests, Peptide Fragments, Sequence Homology, Amino Acid, T-Lymphocytes, Tumor Cells, Cultured