Gamete Recognition in Mice Depends on the Cleavage Status of an Egg’s Zona Pellucida Protein

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Science  09 Jul 2010:
Vol. 329, Issue 5988, pp. 216-219
DOI: 10.1126/science.1188178

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Getting Gametes Together

Despite decades of research, the molecular basis of sperm-egg recognition in mammals remains unresolved. Models in which a glycan ligand in the zona pellucida (ZP) surrounding ovulated eggs binds to a sperm surface receptor have been widely embraced. A more recent model proposes that the cleavage status of a ZP protein, ZP2, renders the structure of the zona matrix either permissive or nonpermissive for sperm binding. Gahlay et al. (p. 216) tested predictions of each model by replacing endogenous zona proteins with either a mutant form of ZP2 that could not be cleaved or of ZP3 that lacked O glycan attachment sites. Sperm-egg recognition depended on the cleavage status of ZP2 rather than on glycan ligands released following fertilization.


At fertilization, mouse sperm bind to the zona pellucida (which consists of glycoproteins ZP1, ZP2, and ZP3) that surrounds eggs. A ZP2 cleavage model of gamete recognition requires intact ZP2, and a glycan release model postulates that zona glycans are ligands for sperm. These two models were tested by replacing endogenous protein with ZP2 that cannot be cleaved (Zp2Mut) or with ZP3 lacking implicated O glycans (Zp3Mut). Sperm bound to two-cell Zp2Mut embryos despite fertilization and cortical granule exocytosis. Contrary to prediction, sperm fertilized Zp3Mut eggs. Sperm at the surface of the zona pellucida remained acrosome-intact for more than 2 hours and were displaced by additional sperm. These data indicate that sperm-egg recognition depends on the cleavage status of ZP2 and that binding at the surface of the zona is not sufficient to induce sperm acrosome exocytosis.

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