l -Fucose utilization provides Campylobacter jejuni with a competitive advantage

Abstract

Campylobacter jejuni is a prevalent gastrointestinal pathogen in humans and a common commensal of poultry. When colonizing its hosts, C. jejuni comes into contact with intestinal carbohydrates, including L-fucose, released from mucin glycoproteins. Several strains of C. jejuni possess a genomic island (cj0480c-cj0490) that is up-regulated in the presence of both L-fucose and mucin and allows for the utilization of L-fucose as a substrate for growth. Strains possessing this genomic island show increased growth in the presence of L-fucose and mutation of cj0481, cj0486, and cj0487 results in the loss of the ability to grow on this substrate. Furthermore, mutants in the putative fucose permease (cj0486) are deficient in fucose uptake and demonstrate a competitive disadvantage when colonizing the piglet model of human disease, which is not paralleled in the colonization of poultry. This identifies a previously unrecorded metabolic pathway in select strains of C. jejuni associated with a virulent lifestyle.pathogenesis | metabolism | gut | mucus

The Human Milk Oligosaccharide 2′-Fucosyllactose Quenches Campylobacter jejuni–Induced Inflammation in Human Epithelial Cells HEp-2 and HT-29 and in Mouse Intestinal Mucosa

“…The binding specificity of C. jejuni varies by strain, and as with the related species Helicobacter pylori (36, 37), C. jejuni has broad binding specificity for mucins and other complex glycans (38,39). In glycan arrays, C. jejuni strain NCTC 11168 binding specificity varies according to growth conditions; under growth conditions mimicking mammalian and avian hosts, NCTC 11168 binds glycans terminating in a-and b-linked galactose and to fucosylated glycans.…”

“…Lewis B and H-2 are the primary glycan moieties recognized (14). Accordingly, high concentrations of L-fucose (39), the fucose binding lectin UEA-I, and the galactose recognizing lectin Ricinus communis agglutinen I (RCA-I) inhibit adherence of C. jejuni strain NCTC 11168 to epithelial cells (15).…”

Modulation of intestinal mucin composition and mucosal morphology by dietary phytogenic inclusion level in broilers

“…Furthermore the changes in mucin monosaccharide composition pattern as in Gal, Fuc and GalNac molar ratios need to be further assessed in terms of overall gut microbial ecology, as it is known that a correlation between mucin composition and bacterial colonization and proliferation exits. The latter is evidenced via the degradation of mucin by bacterial glycosidases (Hoskins et al, 1986;Ruas-Madiedo et al, 2008), the bacterial utilization of mucin carbohydrate side chains as energy source (Salyers, 1979;Scwad and Gä nzle, 2011;Stahl et al, 2011) and the bacterial adhesion in mucin monosaccharide (Kirjavainen et al, 1998;Gusils et al, 2003), as well as the ability of gut microflora to modulate intestinal glycosylation (Bry et al, 1996;Gheri Bryk et al, 1999;Freitas et al, 2005) and mucin gene expression (Mack et al, 1999 and. Therefore, this correlation may determine to a significant extent which species or even strains within species are best suited for utilization, colonization and/or adhesion to intestinal mucus.…”

FdhTU-Modulated Formate Dehydrogenase Expression and Electron Donor Availability Enhance Recovery ofCampylobacter jejunifollowing Host Cell Infection

“…A number of recent studies have also demonstrated the importance of C. jejuni factors modulating metabolism and physiology during the colonization of animal hosts. These include nutrient utilization systems such as the cj0480c-cj0490 operon, allowing C. jejuni to use L-fucose as a growth substrate (69); aspartase, which converts aspartate into both a carbon source and fumarate for respiration (27); and gamma-glutamyl transpeptidase, which converts glutathione into amino acids and glutamine into glutamate, each of which in turn can be used for growth (5,31). Chicken colonization defects were also observed in gluconate dehydrogenase (56) and hydrogenase (hydB) (81) mutant backgrounds, indicating the importance of gluconate and hydrogen gas, respectively, as electron donors in vivo.…”