Genetic Analysis of Monoclonal Antibody and HIV Binding Sites on the Human Lymphocyte Antigen CD4

Overview

Journal Cell

Publisher Cell Press

Specialty Cell Biology

Date 1988 Jul 1

PMID 2454749

Citations 84

Authors

A Peterson

B Seed

Affiliations

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Abstract

Saturation mutagenesis and a complement fixation selection have yielded CD4 point mutants with impaired antibody and human immunodeficiency virus binding. The patterns of amino acid substitution, in conjunction with previous antibody cross-blocking data, affirm the similar tertiary structures of the CD4 amino-terminal domain and immunoglobulin variable regions. Single residue substitutions affecting virus binding and syncytium formation are observed over an eight residue segment located in a portion of the molecule homologous to the second hypervariable region of an antibody combining site.

Citing Articles

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The productive entry pathway of HIV-1 in macrophages is dependent on endocytosis through lipid rafts containing CD4.

van Wilgenburg B, Moore M, James W, Cowley S PLoS One. 2014; 9(1):e86071.

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Reduced monomeric CD4 is the preferred receptor for HIV.

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Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoprotein.

Xiang S, Kwong P, Gupta R, Rizzuto C, Casper D, Wyatt R J Virol. 2002; 76(19):9888-99.

PMID: 12208966 PMC: 136507. DOI: 10.1128/jvi.76.19.9888-9899.2002.