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Glycobiology, 2000, Vol. 10, No. 3 313-320
© 2000 Oxford University Press

A novel viral {alpha}2,3-sialyltransferase (v-ST3Gal I): transfer of sialic acid to fucosylated acceptors

Keiko Sujino, Ronald J. Jackson2, Nora W. C. Chan, Shuichi Tsuji3 and Monica M. Palcic1

Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2, Canada, 2Pest Animal Control CRC, CSIRO Wildlife and Ecology, Canberra ACT 2601, Australia, and 3Laboratory for Molecular Glycobiology, Frontier Research Program, The Institute of Physical and Chemical Research (RIKEN), Hirosawa, Wako, Saitama 351–0198, Japan

The substrate specificity of an {alpha}2,3-sialyltransferase (v-ST3Gal I) obtained from myxoma virus infected RK13 cells has been determined. Like mammalian sialyltransferase enzymes, the viral enzyme contains the characteristic L- and S-sialyl motif sequences in its catalytic domain. Analysis of the deduced amino acid sequences of cloned sialyltransferases suggests that v-ST3Gal I is closely related to mammalian ST3Gal IV. v-ST3Gal I catalyzes the transfer of sialic acid from CMP-NeuAc to Type I (Galß1-3GlcNAcß) II (Galß1-4GlcNAcß) and III (Galß1-3GalNAcß) acceptors. In addition, the viral enzyme also transfers sialic acid to the fucosylated acceptors Lewisx and Lewisa. This substrate specificity is unlike any sialyltransferases described to date, though it is most comparable with those of mammalian ST3Gal IV enzymes. The products from reactions with fucosylated acceptors were characterized by capillary zone electrophoresis, 1H-NMR spectroscopy and mass spectrometry. They were shown to be 2,3-sialylated Lewisx and 2,3-sialylated Lewisa, respectively.

1 To whom correspondence should be addressed


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