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NMR spectroscopy and methylation linkage analysis reveal the presence of the O antigenic polysaccharide found in Campylobacter jejuni and bacterial isolates found in patients who later develop the Guillain-Barre syndrome. The glycan is a hyaluronic acid derivative with beta-D-glucuronic acid residues present as amides of 2-amino-2-deoxyglycerol. A similar structure is seen in Shigella boydii type 8 and Vibrio cholerae strain H11.

The lipopolysaccharide of Campylobacter jejuni has a central region that is homologous to gangliosides due to the presence of two oligosaccharide chains. The first chain has a single N-acetylneuraminic acid residue similar to GM and the second chain has a terminal region resembling GD. Lipopolysaccharide of bacterial isolates from patients with the Guillain-Barre syndrome possess significantly shorter oligosaccharide regions.

Lipopolysacharides (LPS) from antigentically different strains assigned to seroroups O:3 and O:6 of Helicobacter pylori were isolated as water-soluble material of high Mr and as water-insoluble gels of low Mr. Chemical and spectroscopic analyses of the soluble LPS and oligosaccharides liberated from the water-insoluble gels led to proposed structures with Lewis (Le) antigen determinants terminating regular repeating units of different types, linked in turn to inner core regions of invariable structure. The O:6 LPS has two populations of related molecules with chains of 3-linked D-glycero-α-D-manno-heptose residues similar to those in the MO19 strain, one with and the other without a single terminal Lewis (Ley) epitope. In contrast, in the O:3 LPS. Lewis (Lex and Ley epitopes terminate a partially fucosylated N-acetyllactosaminoglycan, but a heptan chain similar to that in the O:6 LS was shown to connect the outer chains to the inner core. These PS provide examples of the molecular mimicry of cell-surface glycoconjugates. Structural variations of LPS between strains, and differences in some aspects of structure within the strains, between high Mr and low Mr LPS indicate a class of LPS whose mechanisms of biosynthesis lead to overall architectures different from those characteristics of most LPS from enteric bacteria. [ABSTRACT FROM AUTHOR]