Antisperm antibody detected in infertile female patients' sera has been shown to correlate with reduced fertility. The antibody showed strong complement-dependent cytotoxicity as determined by the sperm immobilization test (SIT). CD52 is a human glycosylphosphatidylinositol (GPI)-anchored antigen present in lymphocytes and male reproductive tracts (mrt), including mature sperm and seminal plasma. Recently, purified mrt-CD52 from human seminal plasma has been reported to interfere with the classical complement pathway, but not lectin binding or alternative pathways of the complement system. The purpose of this study is to determine which stage of the classical pathway mrt-CD52 regulates. mrt-CD52 was purified from human seminal plasma or intact sperm membrane. Immunoprecipitation assay was performed with the reaction of mrt-CD52, human complement and mAb H6-3C4. Immunoprecipitate was formed by the carbohydrate moiety of mrt-CD52, but not by the GPI-anchor peptide. The C1q molecule (29 kDa) was detected in the immunoprecipitates by Western blotting analysis probed with anti C1q antibody, indicating that the carbohydrate moiety of mrt-CD52 binds to C1q. Also, the complement-dependent SIT revealed that purified CD52 inhibited sperm immobilization activity by antisperm antibody. These results suggest that mrt-CD52 protects sperm function from complement attack if antisperm antibody is generated in the female reproductive tracts.
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