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Originally published In Press as doi:10.1074/jbc.R600001200 on February 1, 2006

J. Biol. Chem., Vol. 281, Issue 20, 13853-13856, May 19, 2006
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Molecular Models for Murine Sperm-Egg Binding*

Gary F. Clark{ddagger}1 and Anne Dell§2

From the {ddagger}Department of Obstetrics, Gynecology and Women's Health, Division of Reproductive and Perinatal Research, School of Medicine, University of Missouri, Columbia, Missouri 65202 and the §Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, United Kingdom

Murine sperm initiate fertilization by binding to the specialized extracellular matrix of mouse eggs, known as the zona pellucida. Over the past decade, powerful genetic, biophysical, and biochemical techniques have been employed to gain new insights into this interaction. Evidence from these studies does not support either of two major models for binding first proposed over two decades ago. Two more recently established models suggest that protein-protein interactions predominate during this initial stage of fertilization. Another model proposes that about 75–80% of the murine sperm bound to zona pellucida under well defined in vitro conditions is carbohydrate dependent, with the remaining sperm bound via protein-protein interactions. Mounting evidence suggests that the carbohydrate sequences coating the murine egg could be employed as specific immune recognition markers. Continued investigation of this system may resolve many of these controversial findings and reveal novel functions for murine zona pellucida glycoproteins.


* This minireview will be reprinted in the 2006 Minireview Compendium, which will be available in January, 2007. Studies cited in this review that were performed by G. F. C. and collaborators were supported by National Institutes of Health Grants HD35652 and AI60397, the Breeden-Adams Foundation, the Elsa U. Pardee Foundation, and the Jeffress Trust. Studies performed by A. D. were supported by the Biotechnology and Biological Sciences Research Council (BBSRC) and the Wellcome Trust.

1 Member of the Consortium for Functional Glycomics supported by the NIGMS of the NIH. To whom correspondence may be addressed. Tel.: 573-882-1725; Fax: 757-624-2269; E-mail: clarkgf{at}health.missouri.edu. 2 BBSRC Professorial Fellow. Member of the Consortium for Functional Glycomics supported by the NIGMS of NIH. To whom correspondence may be addressed. Tel.: 44-207-594-5219; Fax: 44-207-225-0458; E-mail: a.dell{at}imperial.ac.uk.


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