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To assess the antigenicity of envelope glycoproteins derived from primary human immunodeficiency virus type 1 populations, their interactions with the receptor CD4, and their coreceptor usage, we have cloned and expressed multiple gp120 proteins from a number of primary virus isolates. Characterization of these proteins showed a high degree of antigenic polymorphism both within the CD4 binding site and in defined neutralization epitopes, which may partially account for the general resistance of primary isolates to neutralizing agents. Furthermore, chimeric viruses expressing gp120 proteins with reduced CD4 binding abilities are viable, suggesting that primary viruses may require a less avid interaction with the receptor CD4 to initiate infection than do their laboratory-adapted counterparts. The coreceptor usage of chimeric viruses was related to the ability of the virus to bind CD4, with reduced CD4 binding correlating with preferential usage of CXCR4. Changes in coreceptor usage mapped to sequence changes in the C2 and V4 regions, with no changes seen in the V3 region.

Original publication




Journal article


J Virol

Publication Date





5593 - 5603


Amino Acid Sequence, Animals, Antigenic Variation, Binding Sites, CD4 Antigens, HIV Envelope Protein gp120, HIV Infections, HIV-1, Humans, Male, Molecular Sequence Data, Peptide Fragments, Polymerase Chain Reaction, Rats, Receptors, Chemokine, Recombinant Fusion Proteins, Sequence Analysis, DNA