ANTISPERM ANTIBODY-BINDING TO HUMAN SPERM INHIBITS CAPACITATION INDUCED CHANGES IN THE LEVELS OF PLASMA-MEMBRANE STEROLS

PROBLEM: Human spermatozoa express mannose ligand receptors (MLRs) over the entire head when incubated under conditions that promote loss of free cholesterol. Binding of IgA, IgG, and/or IgM head-directed anti-sperm antibodies (ASAs) to freshly isolated sperm blocks MLR expression in a dose dependent manner. METHODS: Comparison of Western blots of immunoprecipated glycoproteins from fresh sperm exposed to ASAs from women with those of sperm membrane proteins isolated from capacitated sperm probed with a goat anti-human macrophage MLR antiserum showed that ASAs do not react with human sperm MLRs of 48 and 61 kd apparent molecular weight. RESULTS: The direct effect of ASA binding was to increase membrane free cholesterol content which remained greater than 0.005 mumol/10(9) sperm after 18 h incubations, whereas the sterol content of controls decreased to less than 0.001 mumol/10(9) sperm. Cholesterol addition to sperm inhibited MLR expression in a manner analogous to ASA binding, while increasing temperatures up to the crystalline/liquid-crystalline phase transition for sperm membranes; less than 45-degrees-C failed to promote the appearance of MLRs on the surface of fresh sperm. CONCLUSIONS: We conclude that ASA effects on membrane cholesterol content prevent the membrane fluidity changes needed for MLR expression.