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Molecular Human Reproduction, Vol. 7, No. 4, 313-317, April 2001
© 2001 European Society of Human Reproduction and Embryology

Commentary

Do fertilin ß and cyritestin play a major role in mammalian sperm-oolemma interactions? A critical re-evaluation of the use of peptide mimics in identifying specific oocyte recognition proteins

Eileen A. McLaughlin, Jan Frayne, Graham Bloomerg and Len Hall,1

Department of Biochemistry, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD, UK

Integrins have been proposed to play a role in mammalian sperm–oocyte interactions for many years. To a large extent this hypothesis stems from the ability of short synthetic peptides, based on the disintegrin-like domains of two sperm surface integral membrane proteins, fertilin ß and cyritestin, to inhibit sperm–oocyte binding and fusion in vitro. Here we argue that such peptide mimics lack specificity in these simple IVF assay systems. Hence, whilst not precluding a role for fertilin ß and cyritestin in sperm–oolemma interactions, this lack of specificity indicates the need for considerable caution when interpreting results obtained using this approach.

ADAM protein/disintegrin/integrin/IVF/MDC protein/sperm-oocyte binding

1 To whom correspondence should be addressed. E-mail: L.Hall{at}bris.ac.uk


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