Lipopolysaccharides of Campylobacter jejuni serotype O:19: structures of O antigen chains from the serostrain and two bacterial isolates from patients with the Guillain-Barré syndrome.

An O antigenic polysaccharide was liberated from the lipopolysaccharide of high M(r) from Campylobacter jejuni serotype O:19 by acetic acid hydrolysis of the ketosidic linkage to lipid A. The structure of the polysaccharide was established in several one- and two-dimensional 1H and 13C NMR experiments, fast atom bombardment mass spectrometry and methylation linkage analysis of the permethylated glycan and its degradation products. It is concluded that the glycan is a derivative of hyaluronic acid in which the beta-D-glucuronic acid residues in the alternating sequence [-4)-beta-D-GlcA-(1-->3)-beta-D-GlcNAc-(1]n are present as amides of 2-amino-2-deoxyglycerol. Parallel experiments were performed on O antigens liberated from lipopolysaccharides of high M(r) from bacterial isolates that had been obtained from two patients who subsequently developed the Guillain-Barré syndrome. Within the limits of structural analysis by NMR spectroscopy and methylation linkage analysis, both these O antigens were identical to that from the serostrain.