Helicobacter pylori is a highly persistent and common pathogen in humans. It is the causative agent of chronic gastritis and its further stages. HP0826 is the β-1,4-galactosyltransferase involved in the biosynthesis of the LPS O-chain backbone of H. pylori. Though it was first cloned nearly a decade ago, there are surprisingly limited data about the characteristics of HP0826, especially given its prominent role in H. pylori pathogenicity. We here demonstrate that HP0826 is a highly efficient and promiscuous biocatalyst. We have exploited two novel enzymatic activities for the quantitative synthesis of the thiodisaccharide Gal-β-S-1,4-GlcNAc-pNP as well as Gal-β-1,4-Man-pNP. We further show that Neisseria meningitidis β-1,4-galactosyltransferases LgtB can be used as an equally efficient catalyst in the latter reaction. Thiodisaccharides have been extensively used in structural biology but can also have therapeutic uses. The Gal-β-1,4-Man linkage is found in the Leishmania species LPG backbone disaccharide repeats and cap, which have been associated with vector binding in Leishmaniasis
specificity, glycosyltransferases, acceptor, kinetics, saccharides, biocatalysis
NCBI PubMed ID: 18491328Publication DOI: 10.1002/cbic.200700775Journal NLM ID: 100937360Publisher: Weinheim, Germany: Wiley Interscience
Correspondence: warren.wakarchuk@nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council Canada, 100 Sussex Drive, Ottawa, ON K1A0R6, Canada
Methods: 13C NMR, 1H NMR, NMR-2D, ESI-MS, genetic methods, biochemical methods, CE
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