Assessment of glycan interactions of clinical and avian isolates of Campylobacter jejuni

Abstract

BackgroundCampylobacter jejuni strain 11168 was demonstrated to have a broad specificity for eukaryotic surface glycosylation using glycan array analysis. The initial screen indicated that sialic acid and mannose are important binding partners after environmental stress, while galactose and fucose structures are likely to be involved in persistent infection.ResultsIn this broader study, five additional human/clinical isolates and six chicken isolates were fully assessed to determine their glycan binding capacity using an extended glycan array. C. jejuni 11168 was rescreened here due to the presence of glycoaminoglycan (GAG) and other structures that were not available on our previous glycan array. The current array analysis of additional C. jejuni strains confirmed the growth condition dependent differences in glycan binding that was previously observed for C. jejuni 11168. We noted strain to strain variations, particularly for the human isolates C. jejuni 520 and 81116 and the chicken isolate C. jejuni 331, with the majority of differences observed in galactose, mannose and GAG binding. Chicken isolates were found to bind to a broader range of glycans compared to the human isolates, recognising branched mannose and carageenan (red seaweed) glycans. Glycan array data was confirmed using cell-based lectin inhibition assays with the fucose (UEA-I) and mannose (ConA) binding lectins.ConclusionsThis study confirms that all C. jejuni strains tested bind to a broad range of glycans, with the majority of strains (all except 81116) altering recognition of sialic acid and mannose after environmental stress. Galactose and fucose structures were bound best by all strains when C. jejuni was grown under host like conditions confirming the likelihood of these structures being involved in persistent infection.

A novelO-linked glycan modulatesCampylobacter jejunimajor outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization

“…The high degree of specificity exhibited by H. pylori in its BgAg-binding interactions [ 28 , 29 ] is in contrast to our findings, and those of Day et al . [ 23 ], showing that C. jejuni can bind to a wide range of related antigens. This may reflect the contrast between the very restricted host range of H. pylori , which infects only humans, and that of C. jejuni , which is able to establish infection in a wide range of birds and mammals.…”

“…Ruiz-Palacios and co-workers [ 21 , 22 ] showed that fucosylated sugar components in human breast milk could inhibit C. jejuni binding to HEp-2 cells in vitro and to human intestinal mucosa ex vivo , and also prevent C. jejuni infection of mice in vivo . Subsequent solid-phase assays confirmed the binding of C. jejuni strains, grown under host-like conditions, to a broad range of fucose (and galactose)-containing glycans, with different strains exhibiting differing binding profiles and avidities [ 21 , 23 ]; however, the identity of the C. jejuni lectin(s) responsible for this binding has not to date been determined. The common ABO histo-blood group antigens (BgAgs) comprise a complex and polymorphic group of fucosylated carbohydrates expressed on the surfaces of erythrocytes, but they are also highly expressed in the oro-gastro-intestinal (OGI) epithelium, as well as endothelial cells, and in secretions, such as milk, saliva and tears [ 24 , 25 ].…”

Avian Intestinal Mucus Modulates Campylobacter jejuni Gene Expression in a Host-Specific Manner

“…These genes have been shown to be necessary for growth on fucose which is an abundant sugar found in mucin (Muraoka and Zhang, 2011), and C. jejuni NCTC11168 is one of several C. jejuni strains known to have this operon and to utilize fucose (Muraoka and Zhang, 2011; Stahl et al, 2011). Strains of C. jejuni from human and avian sources show affinities for fucose, suggesting its importance for persistence in the gut (Day et al, 2013). Despite the broad importance of fucose for colonization of the gut, fucose permease (fucP) knockout mutants have a colonization defect in mammals but not in the avian gut, suggesting additional substrates support C. jejuni colonization of the avian gut (Stahl et al, 2011).…”

A peculiar case of Campylobacter jejuni attenuated aspartate chemosensory mutant, able to cause pathology and inflammation in avian and murine model animals

“…IMS isolated cells were labelled with CFDA-SE and glycan binding profile was analysed as described in Day et al . 56 . Full list of glycan structures see Table S6 .…”