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Glycobiology Advance Access published online on May 26, 2004
Glycobiology, doi:10.1093/glycob/cwh100
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Received April 7, 2004
Revised May 15, 2004
Accepted May 21, 2004

ORIGINAL ARTICLES

A major flagellum sialoglycoprotein in sea urchin sperm contains a novel polysialic acid, an {alpha}2,9-linked poly-N-acetylneuraminic acid chain, capped by an 8-O-sulfated sialic acid residue*

Shinji Miyata 1, Chihiro Sato 2, Shigeyuki Kitamura 1, Masaru Toriyama 3, Ken Kitajima 4*

1 Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
2 Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan; Bioscience and Biotechnology Center, Nagoya University, Nagoya 464-8601, Japan
3 Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Ohya, Shizuoka 422-8529, Japan
4 Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan; Bioscience and Biotechnology Center, Nagoya University, Nagoya 464-8601, Japan; Institute for Advanced Research, Nagoya University, Nagoya 464-8601, Japan

* To whom correspondence should be addressed. E-mail: kitajima{at}agr.nagoya-u.ac.jp.


  Abstract

A new type of polysialic acid (polySia) structure was demonstrated to occur in a major unknown sialoglycoprotein with a diverse molecular mass of 40-80 kDa in sea urchin sperm. The polySia-containing glycan structure was determined to be HSO3->8Neu5Ac{alpha}2->9(Neu5Ac{alpha}2->9)n-2 Neu5Ac{alpha}2->6GalNAc{alpha}1->Ser/Thr (n, on average 15), based on carbohydrate analysis of the sialoglycopeptide obtained by an exhaustive protease digestion of whole sperm, fluorometric anion-exchange high performance liquid chromatography, and methylation analysis. The sulfate group was predominantly localized to the non-reducing terminus of the polySia chain. This is the first example of an {alpha}2,9-linked polySia structure in animal sperm. The polySia-containing sialoglycoprotein was present in sperm flagellum, but not in the head. Furthermore, this sialoglycoprotein localized in the sperm lipid raft, which contains an enriched ganglioside (Neu5Ac{alpha}2->8Neu5Ac{alpha}2->6GlcCer), a receptor for sperm activating peptide (speract), and its associated guanylate cyclase [Ohta et al. (2000) Glycoconjugate J. 17, 205-214].


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