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Bovine Seminal Plasma Proteins PDC-109, BSP-A3, and BSP-30-kDa Share Functional Roles in Storing Sperm in the Oviduct¹

Department of Biomedical Sciences,³ College of Veterinary Medicine, Department of Molecular Biology and Genetics,⁴ Cornell University, Ithaca, New York 14853 Department of Medicine,⁵ University of Montreal and Guy-Bernier Research Center, Maisonneuve-Rosemont Hospital, Montreal, Quebec, Canada H1T 2M4

ABSTRACT

On ejaculation, sperm become coated with proteins secreted by the male accessory sex glands. In the bull, these proteins consist predominantly of the bovine seminal plasma family of proteins (BSPs): PDC-109 (BSP-A1/-A2), BSP-A3, and BSP-30-kDa. PDC-109 plays a role in forming an oviductal sperm reservoir by enabling sperm to bind to oviductal epithelium. Because PDC-109 has high sequence identity with the other BSPs, we tested BSP-A3 and BSP-30-kDa for the capacity to bind sperm to oviductal epithelium. BSP-A3 and BSP-30-kDa each increased binding of epididymal sperm to epithelium and were as effective as PDC-109 in competitively inhibiting binding of ejaculated sperm. Because binding extends the motile life of sperm, BSPs were tested for the ability to maintain sperm motility. BSP-treated epididymal sperm incubated with plasma membrane vesicles from bovine oviductal epithelium maintained progressive motility longer than untreated sperm. To our knowledge, this is the first report of this protective effect of BSPs. Similarities in function among the BSPs were reflected in their three-dimensional structure, whereas surface maps of electrostatic potential indicated differences in binding affinities and kinetics. Such differences may provide sperm with greater adaptability to variations among females. Altogether, these results indicate that BSPs play a crucial role in fertilization by maintaining sperm motility during storage.

fallopian tubes, male reproductive tract, oviduct, sperm, sperm motility and transport

¹ Supported by a Canadian Institutes of Health Research grant to P.M. and by National Research Initiative Competitive Grant no. 2004-35203-14952 from the USDA Cooperative State Research, Education, and Extension Service to S.S.S. The contributions of J.L.M. were supported by grant HD38921 from the National Institutes of Health to M.F. Wolfner.

² Correspondence: Susan S. Suarez, Department of Biomedical Sciences, College of Veterinary Medicine, Cornell University, T5–006 Veterinary Research Tower, Ithaca, NY 14853. FAX: 607 253 3541; sss7{at}cornell.edu

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Biol Reprod 2006 75: 491. [Full Text]