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Glycobiology Advance Access published online on May 28, 2008
Glycobiology, doi:10.1093/glycob/cwn047
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Multifunctionality of Campylobacter jejuni sialyltransferase CstII: Characterization of GD3/GT3 oligosaccharide synthase, GD3 oligosaccharide sialidase and trans-sialidase activities

Jiansong Cheng, Hai Yu, Kam Lau, Shengshu Huang, Harshal A. Chokhawala, Yanhong Li, Vinod Kumar Tiwari and Xi Chen1

Department of Chemistry, University of California, One Shields Avenue, Davis, California 95616, USA

1 To whom correspondence should be addressed; Tel: 1-530-754-6037; Fax: 1-530-752-8995; e-mail: chen{at}chem.ucdavis.edu, xiichen{at}ucdavis.edu

Received on February 2, 2008; accepted on May 22, 2008

CstII from bacterium Campylobacter jejuni strain OH4384 has been previously characterized as a bifunctional sialyltransferase having both {alpha}2,3-sialyltransferase (GM3 oligosaccharide synthase) and {alpha}2,8-sialyltransferase (GD3 oligosaccharide synthase) activities which catalyze the transfer of N-acetylneuraminic acid (Neu5Ac) from CMP-Neu5Ac to C-3’ of the galactose in lactose and to C-8 of the Neu5Ac in 3’-sialyllactose, respectively (Gilbert et al. 2000). We report here the characterization of a truncated CstII mutant (CstII{Delta}32I53S) cloned from a synthetic gene whose codons are optimized for Escherichia coli expression system. In addition to the {alpha}2,3- and {alpha}2,8- sialyltransferase activities reported before for the synthesis of GM3 and GD3 type oligosaccharides respectively, the CstII{Delta}32I53S has {alpha}2,8-sialyltransferase (GT3 oligosaccharide synthase) activity for the synthesis of GT3 oligosaccharide. It also has {alpha}2,8-sialidase (GD3 oligosaccharide sialidase) activity that catalyzes the specific cleavage of the {alpha}2,8-sialyl linkage of GD3 type oligosaccharides and {alpha}2,8-trans-sialidase (GD3 oligosaccharide trans-sialidase) activity that catalyzes the transfer of a sialic acid from a GD3 oligosaccharide to a different GM3 oligosaccharide (3’-sialyllactoside). The donor substrate specificity study of the CstII{Delta}32I53S GD3 oligosaccharide synthase activity indicates that the enzyme is flexible in using different CMP-activated sialic acids and their analogs for the synthesis of GD3 oligosaccharides containing natural and non-natural modifications at the terminal sialic acid.

Key words: CstII / ganglioside / sialidase / sialyltransferase / trans-sialidase


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