ISOLATION AND CHARACTERIZATION OF A NOVEL HUMAN SPERM ANTIGEN (H-SP-1)

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We isolated a human sperm antigen gene (h-sp-1) by screening from human testis cDNA library with human sperm specific antisera. The sequence analysis of the h-sp-1 gene indicated that it contained 2170 bp and had 45% homology to human synaptophysin gene, which was considered to play a crucial role in calcium dependent signal transduction in synaptic vesicles in the terminal end of nerves. The analysis of the deduced amino acids from the h-sp-1 gene showed that it encoded 259 amino acids containing four hydrophilic regions and four hydrophobic regions. This indicated that the molecules encoded by the h-sp-1 gene might be a transmembrane protein with four membrane spanning regions like the synaptophysin. In order to characterize the molecules encoded by the hsp-1 gene, the antisera were generated by immunizing rabbits and mice with synthetic polypeptides (No174-198) based on the h-sp-1 gene. The resultant antisera stained fixed human sperm head by indirect immunofluorescence staining. The purified anti-h-sp-1 antibodies showed the inhibitory effect on human sperm penetration assay into zona-free hamster eggs. However they did not show any sperm immobilizing and agglutinating activities. These results suggested that the molecules encoded by the h-sp-1 gene might play an important role in the sperm-egg interaction.