Beta1 integrin is an adhesion protein for sperm binding to eggs.

We investigated the role of beta(1) integrin in mammalian fertilization and the mode of inhibition of fertilinbeta-derived polymers. We determined that polymers displaying the Glu-Cys-Asp peptide from the fertilinbeta disintegrin domain mediate inhibition of mammalian fertilization through a beta(1) integrin receptor on the egg surface. Inhibition of fertilization is a consequence of competition with sperm binding to the cell surface, not activation of an egg-signaling pathway. The presence of the beta(1) integrin on the egg surface increases the rate of sperm attachment but does not alter the total number of sperm that can attach or fuse to the egg. We conclude that the presence of beta(1) integrin enhances the initial adhesion of sperm to the egg plasma membrane and that subsequent attachment and fusion are mediated by additional egg and sperm proteins present in the beta(1) integrin complex. Therefore, the mechanisms by which sperm fertilize wild-type and beta(1) knockout eggs are different.