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Glycobiology Advance Access originally published online on May 28, 2008
Glycobiology 2008 18(9):686-697; 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 Cheng2, Hai Yu2, Kam Lau2, Shengshu Huang2, Harshal A Chokhawala2, Yanhong Li2, Vinod Kumar Tiwari2 and Xi Chen1,2

2 Department of Chemistry, University of California, One Shields Avenue, Davis, CA 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

Received on February 2, 2008; revised on May 17, 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 cytidine 5'-monophosphate (CMP)-Neu5Ac to C-3' of the galactose in lactose and to C-8 of the Neu5Ac in 3'-sialyllactose, respectively (Gilbert M, Karwaski MF, Bernatchez S, Young NM, Taboada E, Michniewicz J, Cunningham AM, Wakarchuk WW. 2002. The genetic bases for the variation in the lipo-oligosaccharide of the mucosal pathogen, Campylobacter jejuni. Biosynthesis of sialylated ganglioside mimics in the core oligosaccharide. J Biol Chem. 277:327–337). We report here the characterization of a truncated CstII mutant (CstII{Delta}32I53S) cloned from a synthetic gene whose codons are optimized for an 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 nonnatural modifications at the terminal sialic acid.

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


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