Lipooligosaccharide of Campylobacter jejuni: similarity with multiple types of mammalian glycans beyond gangliosides.
Autor(es): Houliston R. Scott; Vinogradov Evgeny; Dzieciatkowska Monika; Li Jianjun; St Michael Frank; Karwaski Marie-France; Brochu Denis; Jarrell Harold C; Parker Craig T; Yuki Nobuhiro; Mandrell Robert E.; Gilbert Michel
Resumo: Campylobacter jejuni is well known for synthesizing ganglioside mimics within the glycan component of its lipooligosaccharide (LOS), which have been implicated in triggering Guillain-Barré 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-Barré syndrome-associated strain, expresses an unusual sialic acid-containing hybrid oligosaccharide with similarity to both ganglio and Pk 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.
Imprenta: The Journal of Biological Chemistry, v. 286, n. 14, p. 12361-12370, 2011
Identificador do objeto digital: 10.1074/jbc.M110.181750
Descritores: Guillain-Barre Syndrome - Biosynthesis ; Guillain-Barre Syndrome - Proteins
Data de publicação: 2011