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Biology of Reproduction 66, 1193-1202 (2002)
© 2002 Society for the Study of Reproduction, Inc.

Regular Article

Analysis of the Roles of RGD-Binding Integrins, {alpha}4/{alpha}9 Integrins, {alpha}6 Integrins, and CD9 in the Interaction of the Fertilin ß (ADAM2) Disintegrin Domain with the Mouse Egg Membrane1

Xiaoling Zhu a, and Janice P. Evans2,a

a Department of Biochemistry and Molecular Biology, Division of Reproductive Biology, Johns Hopkins University, Bloomberg School of Public Health, Baltimore, Maryland 21205

Fertilin ß (also known as ADAM2), a mammalian sperm protein that mediates gamete cell adhesion during fertilization, is a member of the ADAM protein family whose members have disintegrin domains with homology to integrin ligands found in snake venoms. Fertilin ß utilizes an ECD sequence within its disintegrin domain to interact with the egg plasma membrane; the Asp is especially critical. Based on what is known about different integrin subfamilies and their ligands, we sought to characterize fertilin ß binding sites on mouse eggs, focusing on integrin subfamilies that recognize short peptide sequences that include an Asp residue: the {alpha}5/{alpha}8/{alpha}v/{alpha}IIb or RGD-binding subfamily ({alpha}5ß1, {alpha}8ß1, {alpha}Vß1, {alpha}Vß3, {alpha}Vß5, {alpha}Vß6, {alpha}Vß8, and {alpha}IIbß3) and the {alpha}4/{alpha}9 subfamily ({alpha}4ß1, {alpha}9ß1, and {alpha}4ß7). We tested peptide sequences known to perturb interactions mediated by these integrins in two different assays for fertilin ß binding. Peptides with the sequence MLDG, which perturb {alpha}4/{alpha}9 integrin-mediated interactions, significantly inhibit fertilin ß binding to eggs, which suggests a role for a member of this integrin subfamily as a fertilin ß receptor. RGD peptides, which perturb {alpha}5/{alpha}8/{alpha}v/{alpha}IIb integrin-mediated interactions, have partial inhibitory activity. The anti-{alpha}6 antibody GoH3 has little or no inhibitory activity. An antibody to the integrin-associated tetraspanin protein CD9 inhibits the binding of a multivalent presentation of fertilin ß (immobilized on beads) but not soluble fertilin ß, which we speculate has implications for the role of CD9 in the strengthening of fertilin ß-mediated cell adhesion but not in initial ligand binding.

First decision: 5 November 2001.

1 This research was supported by grant HD 37696 from the National Institutes of Health (NIH) and by a Faculty Innovation Award from the Johns Hopkins Bloomberg School of Public Health. X.Z. was supported by NIH training grant HD 07276.

2 Correspondence: Janice P. Evans, Division of Reproductive Biology, Department of Biochemistry and Molecular Biology, Johns Hopkins University, Bloomberg School of Public Health, 615 N. Wolfe St., Room 3606, Baltimore, MD 21205. FAX: 410 614 2356; jpevans{at}jhsph.edu




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