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J. Biol. Chem., Vol. 279, Issue 6, 4346-4357, February 6, 2004

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Functional Characterization of Drosophila Sialyltransferase^*

Kate Koles, Kenneth D. Irvine, and Vladislav M. Panin¶

From the Department of Biochemistry and Biophysics, Texas A & M University, College Station, Texas 77843 and Howard Hughes Medical Institute, Waksman Institute, and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854

Sialylation is an important carbohydrate modification of glycoconjugates in the deuterostome lineage of animals. By contrast, the evidence for sialylation in protostomes has been scarce and somewhat controversial. In the present study, we characterize a Drosophila sialyltransferase gene, thus providing experimental evidence for the presence of sialylation in protostomes. This gene encodes a functional 2-6-sialyltransferase (SiaT) that is closely related to the vertebrate ST6Gal sialyltransferase family, indicating an ancient evolutionary origin for this family. Characterization of recombinant, purified Drosophila SiaT revealed a novel acceptor specificity as it exhibits highest activity toward GalNAc1-4GlcNAc carbohydrate structures at the non-reducing termini of oligosaccharides and glycoprotein glycans. Oligosaccharides are preferred over glycoproteins as acceptors, and no activity toward glycolipid acceptors was detected. Recombinant Drosophila SiaT expressed in cultured insect cells possesses in vivo and in vitro autosialylation activity toward -linked GalNAc termini of its own N-linked glycans, thus representing the first example of a sialylated insect glycoconjugate. In situ hybridization revealed that Drosophila SiaT is expressed during embryonic development in a tissue- and stage-specific fashion, with elevated expression in a subset of cells within the central nervous system. The identification of a SiaT in Drosophila provides a new evolutionary perspective for considering the diverse functions of sialylation and, through the powerful genetic tools available in this system, a means of elucidating functions for sialylation in protostomes.

Received for publication, September 5, 2003 , and in revised form, November 10, 2003.

^* This work was supported in part by the Texas Advanced Research Program from the Texas Higher Education Coordinating Board Grant 000517-0069-2001 (to V. M. P.), National Institutes of Health Grant R01-GM54594 (to K. D. I.), and start-up funds from Texas A & M University (to V. M. P.). 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.

^¶ To whom correspondence should be addressed: Dept. of Biochemistry and Biophysics, Texas A & M University, TAMU 2128, College Station, TX 77843-2128. Tel.: 979-458-4630; Fax: 979-862-4718; E-mail: panin{at}tamu.edu.

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