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A Monoclonal Antibody to Human SP-10 Inhibits In Vitro the Binding of Human Sperm to Hamster Oolemma but Not to Human Zona Pellucida

^a Department of Obstetrics and Gynecology, School of Medicine, Keio University, Tokyo 160-8582, Japan ^b Department of Obstetrics and Gynecology, The Saiseikai Central Hospital, Tokyo 108-0073, Japan

SP-10 is a sperm intra-acrosomal protein, specific to the testis, that is believed to play an important role in egg-sperm binding. While the molecular characterization of the SP-10 protein has been clarified, little is yet known of its functional role in fertilization. We therefore established a monoclonal antibody (mAb pep-SP10) against a peptide (pep-SP10) that included the most hydrophilic portion of human SP-10 between the 135th and 149th amino acids. Human SP-10 was found to be localized in the equatorial region of acrosome-reacted sperm by immunofluorescent staining using our mAb pep-SP10. Monoclonal Ab pep-SP10 inhibited sperm-oolemma binding in the zona-free hamster egg penetration test, but it did not inhibit sperm-zona binding in the hemizona assay. Furthermore, we demonstrated that the oolemmal ligands of human SP-10 did not include ß₁ integrins, the most promising candidates for oocyte ligands involved in sperm-oolemma binding, based on the findings of a human sperm-cultured cell binding assay using F9 mouse embryonal carcinoma cells and F9-transformed cells lacking ß₁ integrins. In conclusion, our present data suggest that human SP-10, expressed on the equatorial region of acrosome-reacted sperm, indeed mediates sperm-oolemma binding in a ß₁ integrin-independent manner, but not sperm-zona binding.

First decision: 16 November 1999.

¹ Correspondence and current address: Kiyoo Tanabe, Department of Obstetrics and Gynecology, Tokyo Dental College Ichikawa General Hospital, 5-11-13 Sugano, Ichikawa-city, Chiba 272-8513, Japan. FAX: 81 47 325 4456; ktanabe{at}tdc.ac.jp

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