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Expression of Recombinant Human Zona Pellucida Protein 2 and Its Binding Capacity to Spermatozoa

^a Department of Obstetrics and Gynecology, ^b Laboratory of Developmental Biology and Reproduction, Institute of Advanced Medical Sciences, Hyogo College of Medicine, Nishinomiya, 663-8501, Japan

The human zona pellucida (ZP) is composed of three major glycoproteins: ZP1, ZP2, and ZP3. The aim of this study was to clarify the role of ZP2 by focusing on the polypeptide structure. We produced in Escherichia coli a recombinant human ZP2 protein (rec-hZP2) corresponding to amino acid sequence 1–206 of the mature protein. The final yield of rec-hZP2 protein was 80 µg/ml Luria Broth medium. After 2-h incubation of human spermatozoa with rec-hZP2 in vitro, an immunofluorescent study indicated that rec-hZP2 bound only to acrosome-reacted spermatozoa. The binding site migrated from the acrosome to the midpiece of the spermatozoa. Rabbit and mouse antisera produced against rec-hZP2 stained native human ZP in the immunofluorescent study, and significantly blocked human sperm binding and penetration into human ZP as compared to control values. The N-terminal polypeptide portion of human ZP2 was shown to contain a binding site for acrosome-reacted spermatozoa and to play an important role in secondary sperm binding and penetration into the ZP.

¹ Correspondence: Koji Koyama, Department of Obstetrics and Gynecology, Hyogo College of Medicine, Mukogawa 1–1, Nishinomiya, 663-8501, Japan. FAX: 81 798 46 4163; kkoyama{at}hyo-med.ac.jp

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