Identification of a sialate-O-acetyltransferase from Campylobacter jejuni: demonstration of direct transfer to the C9 position of terminal alpha-2,8-linked sialic acid: J.Biol.Chem.

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TypeArticle
Journal titleJournal Of Biological Chemistry
Volume281
Pages1148011486; # of pages: 7
SubjectACID; biosynthesis; Campylobacter; Campylobacter jejuni; Canada; ENZYME; Escherichia; Escherichia coli; ESCHERICHIA-COLI; GANGLIOSIDE; Gangliosides; Guillain-Barre Syndrome; IDENTIFICATION; lipooligosaccharide; Prevalence; RESIDUES; SIALIC; SIALIC-ACID; SPECIFICITY; STRAIN; STRAINS; structure; Syndrome; transfer
AbstractWe have identified a sialate-O-acetyltransferase in the lipo-oligosaccharide biosynthesis locus of Campylobacter jejuni. Strains possessing this locus are known to produce sialylated outer core structures that mimic host gangliosides, and have been implicated in triggering the onset of Guillain-Barre syndrome. The acetyltransferase, which was cloned and expressed as a fusion construct in Escherichia coli, is soluble and homologous with members of the NodL-LacA-CysE family of O-acetyltransferases. This enzyme catalyzes the transfer of O-acetyl groups onto oligosaccharide-bound sialic acid, with a high specificity for terminal a2,8-linked residues. The modification is directed to C9, and not C7, as is believed to occur more commonly in other organisms. Despite their wide prevalence and importance in both eukaryotes and prokaryotes, this is the first report to describe the characterization of a purified sialate-O-acetyltransferase
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberHOULISTON2006
NPARC number9379851
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Record identifier8f171bae-f791-4619-886b-f808c328e570
Record created2009-07-10
Record modified2016-05-09
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