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We have probed the structure of the C4 and V3 domains of human immunodeficiency virus type 1 gp120 by immunochemical techniques. Monoclonal antibodies (MAbs) recognizing an exposed gp120 sequence, (E/K)VGKAMYAPP, in C4 were differentially sensitive to denaturation of gp120, implying a conformational component to some of the epitopes. The MAbs recognizing conformation-sensitive C4 structures failed to bind to a gp120 mutant with an alteration in the sequence of the V3 loop, and their binding to gp120 was inhibited by both V3 and C4 MAbs. This implies an interaction between the V3 and C4 regions of gp120, which is supported by the observation that the binding of some MAbs to the V3 loop was often enhanced by amino acid changes in an around the C4 region.


Journal article


Journal of virology

Publication Date





4785 - 4796


Aaron Diamond AIDS Research Center, New York University School of Medicine, New York 10016.


Cells, Cultured, Animals, Humans, Mice, HIV-1, Recombinant Proteins, HIV Envelope Protein gp120, Antibodies, Monoclonal, Binding Sites, Antibody, Epitopes, Binding, Competitive, Amino Acid Sequence, Protein Conformation, Kinetics, Models, Structural, Molecular Sequence Data, Genetic Variation