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Abstract
Human semen is the main vehicle for the transmission of human immunodeficiency virus (HIV); therefore, the interaction of HIV with the sperm is worthy of study. The motile sperm head fixation method was used as an in vitro model system to demonstrate the interaction of sperm with the peptide of HIV envelope protein. A micropipette loaded with semen was put into phosphate-buffered saline (PBS) containing V3 peptide (HIV-1 IIIB envelope protein, fragment 307–330) or C2 peptide (HIV-1 IIIB envelope protein, fragment 254–274). The V3 peptide caused a significant number of head-to-head binding sperm while the C2 peptide did not. This V3 peptide carries a high positive charge, which may overcome the electrostatic resistance on the cell to bring the sperm together. An HIV-CD4+ cell attachment inhibitor, dextran sulfate (DS, molecular weight about 5000), enhanced the sperm head agglutination induced by the V3 peptide. DS is presumed able to bind with specific sites near the V3 domain of gpl20 to induce conformational change so as to prevent the binding of anti-V3 monoclonal antibodies or CD4+ cells to the V3 domain. This study suggests that DS interacts directly with the V3 peptide to enhance the sperm head agglutination.