Campylobacter jejuni is well known for synthesizing ganglioside mimics within the glycan component of its lipooligosaccharide (LOS), which have been implicated in triggering Guillain-Barre syndrome. We now confirm that this pathogen is capable of synthesizing a much broader spectrum of host glycolipid/glycoprotein mimics within its LOS. P blood group and paragloboside (lacto-N-neotetraose) antigen mimicry is exhibited by RM1221, a strain isolated from a poultry source. RM1503, a gastroenteritis-associated strain, expresses lacto-N-biose and sialyl-Lewis c units, the latter known as the pancreatic tumor-associated antigen, DU-PAN-2 (or LSTa). C. jejuni GC149, a Guillain-Barre syndrome-associated strain, expresses an unusual sialic acid-containing hybrid oligosaccharide with similarity to both ganglio and P(k) antigens and can, through phase variation of its LOS biosynthesis genes, display GT1a or GD3 ganglioside mimics. We show that the sialyltransferase CstII and the galactosyltransferase CgtD are involved in the synthesis of multiple mimic types, with LOS structural diversity achieved through evolving allelic substrate specificity.
Lipooligosaccharide, Campylobacter jejuni, gangliosides, mimicry
NCBI PubMed ID: 21257763Publication DOI: 10.1074/jbc.M110.181750Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: michel.gilbert@nrc-cnrc.gc.ca
Institutions: From the Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada
Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, sugar analysis, 31P NMR, NMR-1D, genetic methods, de-N-O-acylation, CE, LC-MS
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