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a Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599
Zonadhesin is a multiple-domain transmembrane protein that is believed to function as a sperm-zona pellucida binding protein. In this study we sequenced zonadhesin from rabbit testis and analyzed its processing, expression, localization, and zona pellucida binding. We show that the precursor protein occurs exclusively in the testis and that proteolytic processing results in the formation of three fragments: p43 (D1 domain), p97 (D2–D4 domains), and p58 (D4 domain-C-terminal). In mature spermatozoa the p43 and p97 fragments exist as disulfide-bonded dimers. During spermatogenesis, synthesis of zonadhesin mRNA chiefly occurs in primary spermatocytes, whereas the protein is abundant in both Sertoli cells and spermatids. In spermatozoa the protein is localized exclusively to the anterior acrosome but is not available for binding antibody on live spermatozoa. Once the acrosome reaction is induced, zonadhesin is lost from the spermatozoon, but remains with the acrosomal shroud. We show that recombinant D4 domain can bind zona pellucida, and we propose that zonadhesin functions after the acrosome reaction has been initiated to bind the acrosomal shroud to the zona pellucida.
1 Support was provided by a National Institutes of Health (NIH) grant and a postdoctoral fellowship through the Center for Recombinant Gamete Vaccinogens, University of Virginia, and the U.S. Public Health Service (U54HD29099) to I.A.L.; and by CONRAD and the NIH International Training and Research Program in Population and Health to P.S.
2 Correspondence: Isabel A. Lea, Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, 210 Taylor Hall, CB 7090, Chapel Hill, NC 27599. FAX: 919 966 1856; ialea{at}email.unc.edu
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