Sperm-associated protein candidates for primary zona pellucida-binding molecules: structure-function correlations of boar spermadhesins.
The initial binding of mammalian spermatozoa and the zona pellucida of their homologous oocytes appears to be mediated by a protein-carbohydrate recognition mechanism. Subsequent protein-protein interaction triggers the acrosome reaction leading to sperm penetration. Spermatozoa possess a complement of surface-associated proteins that mediate interactions with the zona pellucida of the oocyte at fertilization. Both integral membrane and peripherally associated zona pellucida-interacting molecules have been described in a number of species. Some of these proteins have been shown to possess carbohydrate-binding activity and are therefore classified as candidates for primary gamete recognition molecules. The participation of any of these proteins in the in vivo situation is, however, a matter of debate. Here, we summarize current knowledge of the most thoroughly studied sperm-associated zona pellucida- and carbohydrate-binding molecules, paying special attention to recent evidence from our laboratories for considering sperm-adhesin AWN, and probably other members of its protein family, as a bona fide candidate for the primary gamete adhesion lectin.
Töpfer-Petersen
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Institut für Reproduktionsmedizin, Tierärztliche Hochschule, Hannover, Germany.
Calvete
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D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D005260:Female; D006801:Humans; D008297:Male; D051379:Mice; D011817:Rabbits; D029589:Seminal Plasma Proteins; D013084:Sperm-Ovum Interactions; D013094:Spermatozoa / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013552:Swine / Q000378:metabolism*; D015044:Zona Pellucida / Q000378:metabolism*
D002352:Carrier Proteins; D029589:Seminal Plasma Proteins; C425042:spermadhesin