IMR Press / FBL / Volume 12 / Issue 5 / DOI: 10.2741/2186

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Article
New insights into sperm-zona pellucida interaction: involvement of sperm lipid rafts
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1 Hormones/Growth/Development, Ottawa Health Research Institute, and Department of Biochemistry/Microbiology/Immunology, University of Ottawa, Ottawa, Ontario, Canada
2 Department of Obstetrics and Gynecology, University of Ottawa, Ottawa, Ontario, Canada
3 Centre de Recherche Guy-Bernier, Hôpital MaisonneuveRosemont, Department of Medicine, University of Montreal, Montreal, Canada
4 Department of Animal Science, University of California, Davis, California, U.S.A.
5 Center for Research on Reproduction and Women's Health, Department of Obstetrics and Gynecology, University of Pennsylvania Medical Center, Pennsylvania, U.S.A.
Front. Biosci. (Landmark Ed) 2007, 12(5), 1748–1766; https://doi.org/10.2741/2186
Published: 1 January 2007
Abstract

Sperm-zona pellucida (ZP) binding is the first step of gamete interaction. This binding occurs in two sequential steps, starting with the primary binding of acrosome-intact sperm to the ZP followed by the secondary ZP binding of acrosome reacting/reacted sperm. While there are only a few ZP sulfoglycoproteins involved in these binding events, a large number of sperm surface molecules have been shown to possess ZP affinity. In this review, we have given explanations to the existence of these many ZP binding molecules. We have also summarized their origin and the mechanisms of how they are targeted to the sperm surface and acrosome. Recently, we have shown that sperm lipid rafts have affinity for the ZP. A number of ZP binding molecules are also present in sperm lipid rafts. In this review, we have provided an argument that sperm lipid rafts may be the platforms on the sperm surface for ZP interaction.

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