Open AccessGlucosylated N-acetyllactosamine O-antigen chain in the lipopolysaccharide from Helicobacter pylori strain UA861
Author(s) -
Mário A. Monteiro,
David A. Rasko,
Diane E. Taylor,
Malcolm B. Perry
Publication year - 1998
Publication title -
glycobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.757
H-Index - 128
eISSN - 1460-2423
pISSN - 0959-6658
DOI - 10.1093/glycob/8.1.107
Subject(s) - helicobacter pylori , lipopolysaccharide , epitope , chemistry , antigen , strain (injury) , residue (chemistry) , beta (programming language) , microbiology and biotechnology , stereochemistry , biochemistry , biology , immunology , genetics , anatomy , computer science , programming language
The O-antigen chain from the lipopolysaccharide of Helicobacter pylori strain UA861 was determined to be composed of an elongated type 2 N -acetyllactosamine backbone, -[-->3)-beta-D-Gal-(1-->4)-beta-D-GlcNAc-(1-]n-->, with approximately half of the GlcNAc units carrying a terminal alpha-d-Glc residue at the O -6 position. The O-chain of H.pylori UA861 was terminated by a N -acetyllactosamine [beta-D-Gal-(1-->4)-beta-D-GlcNAc] (LacNAc) epitope and did not express terminal Lewis X or Lewis Y blood-group determinants as previously found in other H.pylori strains. The absence of terminal Lewis X and Lewis Y blood-group epitopes and the replacement of Fuc by Glc as a side chain in the O-chain of H.pylori UA861 represents yet another type of lipopolysaccharide structure from H.pylori species. These structural differences in H.pylori lipopolysaccharide molecules carry implications with regard to possible different pathogenic events between strains and respective hosts.