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We have purified a sperm membrane protein, designated
zonadhesin, that binds in a species-specific manner to the
extracellular matrix (zona pellucida) of the egg, and cloned its cDNA.
The cDNA encodes a novel protein with a single transmembrane segment
separating a 36 amino acid, highly basic intracellular C terminus from
a 2418-amino acid extracellular region. The extracellular sequence
specifies a mosaic protein comprising a unique N-terminal domain, a
mucin-like domain, and five tandem domains proximal to the membrane
that are homologous to prepro von Willebrand factor. The N-terminal and
mucin-like domains were absent from zonadhesin that bound to the egg
extracellular matrix, suggesting that processing occurs during sperm
maturation and/or capacitation. By Northern blotting and in situ hybridization, zonadhesin mRNA was detected only within the
testis, where it was expressed primarily in haploid spermatids. The
unique domain structure of zonadhesin suggests multiple functions, one
of which is to mediate sperm adhesion to the zona pellucida.
Volume 270,
Number 44,
Issue of November 3, 1995 pp. 26025-26028
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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