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J. Biol. Chem., Vol. 278, Issue 43, 42050-42057, October 24, 2003

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Identification of the Sea Urchin 350-kDa Sperm-binding Protein as a New Sialic Acid-binding Lectin That Belongs to the Heat Shock Protein 110 Family

IMPLICATION OF ITS BINDING TO GANGLIOSIDES IN SPERM LIPID RAFTS IN FERTILIZATION^*

Eri Maehashi, Chihiro Sato, Kaoru Ohta, Yoichiro Harada, Tsukasa Matsuda, Noritaka Hirohashi¶||, William J. Lennarz¶, and Ken Kitajima**

From the Graduate School of Bioagricultural Sciences, the Bioscience and Biotechnology Center, and the ^**Institute for Advanced Research, Nagoya University, Nagoya 464-8601 and the ^¶Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, New York 11794-5215

The 350-kDa sperm-binding protein (SBP), a species-specific sperm-binding protein, is localized in the vitelline layer of sea urchin eggs. In this study, we have shown for the first time that sperm gangliosides are ligands for the intact glycosylated SBP. Using recombinant fragments of the SBP, the N-terminal heat shock protein 110-like domain was shown to be responsible for the binding. The intact SBP could bind various gangliosides, and the binding was sialidase-sensitive and inhibited by sialyllactose, thus indicating that it is the sialic acid-binding protein. Calcium and magnesium ions were not required but they did enhance the binding activity of SBP. The observation that bacterially expressed recombinant SBP and the sialidase-treated intact glycosylated SBP lost divalent cation-dependent enhancement of binding activity suggests that the sialylated carbohydrate moieties of the SBP may be involved in this property. Furthermore, the SBP was shown to bind sperm lipid rafts, in which gangliosides are enriched, and this binding was lost upon sialidase treatment of the lipid rafts. Finally, liposomes containing the ganglioside specifically inhibited fertilization. Taken together, these results allow us to identify SBP as a member of a new class of sialic acid-binding lectin belonging to the Hsp110 family, and indicate that SBP may be involved in interaction of sperm with the vitelline layer of the egg.

Received for publication, July 12, 2003 , and in revised form, August 12, 2003.

^* This research was supported in part by grants-in-aid for the 21st Century COE Program (to K. K.) and for CREST of Japan Science and Technology Corporation (to K. K.), for Scientific Research (C) (15570096) (to K. K.), and for Young Scientists (B) (14780471) from the Ministry of Education, Science, Sports and Culture (to C. S.), and Mizutani Foundation (to C. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| Present address: Dept. of Biology, Ochanomizu University, Ohtsuka, Tokyo 112-8610, Japan.

To whom correspondence should be addressed. Fax: 81-52-789-4297; E-mail: kitajima{at}agr.nagoya-u.ac.jp.

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