Molecular cloning of the human and monkey sperm surface protein PH-20.
نویسندگان
چکیده
The guinea pig sperm surface protein PH-20 has an essential function in sperm adhesion to the zona pellucida of guinea pig eggs. Fully effective contraception has been achieved by immunizing either male or female guinea pigs with purified guinea pig PH-20. Here we report the isolation of human and cynomolgus monkey PH-20 cDNAs as a key step toward testing the function of primate PH-20 and the contraceptive efficacy of PH-20 immunization in primates. The deduced amino acid sequence of human PH-20 has 509 residues and is 59% identical with guinea pig PH-20, suggesting they may have a conserved function and immunogenicity. Southern blots show that there is a single PH-20 gene in the human genome and Northern blots of human testis poly(A)+ RNA show a 2.4-kb message. Northern blots of tissues other than testis are negative for PH-20, indicating that human PH-20 is testis-specific.
منابع مشابه
cDNA cloning reveals the molecular structure of a sperm surface protein, PH-20, involved in sperm-egg adhesion and the wide distribution of its gene among mammals
Sperm binding to the egg zona pellucida in mammals is a cell-cell adhesion process that is generally species specific. The guinea pig sperm protein PH-20 has a required function in sperm adhesion to the zona pellucida of guinea pig eggs. PH-20 is located on both the sperm plasma membrane and acrosomal membrane. We report here the isolation and sequence of a full-length cDNA for PH-20 (available...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 90 21 شماره
صفحات -
تاریخ انتشار 1993