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Immunoglobulin variable region genes from non-human primates, cynomolgus macaques, were shown to have 85%-98% homology with human immunoglobulin sequences and yet macaques are phylogenetically distant enough to respond against conserved human antigens. Immunoglobulin genes were isolated from monkeys immunized with human CD4 antigen and a human/monkey chimeric anti-CD4 antibody with 91-92% homology to human immunoglobulin framework regions was cloned and expressed. The antibody has an apparent affinity of 3.2 x 10(-11) M and exhibits potent immunosuppressive properties in vitro.

This study was undertaken to analyze the specificity and neutralizing properties of cross-reactive anti-gpl20 antibodies (Abs) in the sera of two human immunodeficiency virus (HIV)-infected asymptomatic individuals. Two panels of murine monoclonal anti-idiotype Abs (anti-id MAbs) were established against cross-reactive polyclonal anti-gpl20 Abs purified from HIV+ sera by sequential affinity chromatography using gpl20sand gpl2OMB-Sepharose columns. These panels of anti-id MAbs were then used to affinity purify idiotype-positive (Id') anti-gpl20 Abs from HIV+ sera. The recovery of each of these Id' Abs by purification indicated that several idiotypically distinct cross-reactive anti-gpl20 Abs are present in sera over a wide range of concentrations. Immunological and biological studies showed that although all of the Id' Abs were reactive

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