Reactivity of antisera to endogenous primate retrovirus with a human T cell membrane protein: recognition of a nonviral glycoprotein by antibodies directed only against carbohydrate components.

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Abstract
A glycosylated protein of approximately 70,000 daltons (gp70) from the surface of human peripheral blood T cells was immunoprecipitated by antisera to the baboon endogenous retrovirus (BEV-M7) and the serologically related feline endogenous retrovirus (RD114) but not by antisera to other retroviruses. Whereas preliminary absorption experiments were consistent with a possible viral specificity for this reaction, detailed biochemical and serologic characterization of the purified cellular protein suggested that it was not related to the gp70 of either M7 or RD114 viruses. The specificity of the reaction was further analyzed by assays of cellular gp70 antigenicity after exposure to exo- and endoglycosidases or trypsin and carbohydrate hapten inhibition studies. The results of these experiments were consistent with the interpretation that the glycoprotein was being recognized by antibody binding to the carbohydrate moiety of the molecule. These results provide an example of an antibody activity that could lead to inappropriate conclusions when sensitive radioimmunoprecipitation techniques are used for the biochemical analysis of antigenic systems. They emphasize the necessity of purifying cellular antigens as a prerequisite to determining the exact basis for a serologic reaction.