Pathogenesis of enteric Campylobacter infection

Vliet, Arnoud H. M. van; Ketley, Julian M.

doi:10.1046/j.1365-2672.2001.01353.x

Cited by 126 publications

(139 citation statements)

References 113 publications

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“…At the beginning of the infection, C. jejuni colonizes the small intestine before moving to the colon, which represents the target organ. C. jejuni is generally considered to be invasive; the level of invasiveness varies depending on the strain (Black et al, 1988;van Vliet & Ketley, 2001). In contrast to the infection of humans, C. jejuni is only a commensal organism in chickens and other birds, where the pathogen preferentially resides in the caecum, which contains many anaerobic fermentative bacteria (Barnes et al, 1972;Lu et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Sulphite : cytochrome c oxidoreductase deficiency in Campylobacter jejuni reduces motility, host cell adherence and invasion

et al. 2011

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Campylobacter jejuni lacks the enzyme phosphofructokinase and, consequently, is incapable of metabolizing glucose. Instead, the pathogen uses a number of other chemicals to serve as electron donors. Like chemolithotrophic bacteria, C. jejuni is able to respire sulphite in the presence of a sulphite : cytochrome c oxidoreductase (SOR) that is encoded by the genes cj0004c and cj0005c; the former encodes a monohaem cytochrome c oxidoreductase and the latter a molybdopterin oxidoreductase. After screening of a transposon-based mutant library, we identified a mutant with an insertion in gene cj0005c that was strongly reduced in its capacity to infect Caco2 cells. Further characterization of a corresponding non-random knockout mutant together with a complemented mutant and the parental strain showed the cj0005c-deficient mutant to exhibit clearly reduced motility and diminished adherence to host cells. Furthermore, the transcription of genes responsible for the synthesis of, in particular, legionaminic acid was downregulated and the mutant had a reduced capacity to autoagglutinate. In contrast, neither the proliferation of the mutant, nor its intracellular ATP content, was altered compared to the parental strain.

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Section: Introductionmentioning

confidence: 99%

Sulphite : cytochrome c oxidoreductase deficiency in Campylobacter jejuni reduces motility, host cell adherence and invasion

et al. 2011

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“…Campylobacter jejuni is the leading cause of bacterial foodborne enteritis in the developed world (55). It is a commensal organism in the intestine of warm-blooded animals and birds (31).…”

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Utilization of Lactoferrin-Bound and Transferrin-Bound Iron by Campylobacter jejuni

et al. 2008

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“…The consumption of contaminated food or water is the usual route for bacterial acquisition. Due to a high and increasing frequency of infection, C. jejuni is of major health and economic importance (50). In contrast to those of many other enteric pathogens, the biology of C. jejuni and the pathophysiology of Campylobacter-mediated disease remain poorly understood (50).…”

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confidence: 99%

“…Until recently, C. jejuni was believed to produce either LPS or LOS. However, repeating oligosaccharide units once considered to be an LPS-associated O-chain are now believed to be capsular (18,50), and there is also a considerable level of surface protein glycosylation (47). Thus, although there is a greater capacity for polysaccharide biosynthesis than previously supposed, C. jejuni may only express LOS and not LPS.…”

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Characterization of theCampylobacter jejuniHeptosyltransferase II Gene,waaF, Provides Genetic Evidence that Extracellular Polysaccharide Is Lipid A Core Independent

et al. 2002

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Campylobacter jejuni produces both lipooligosaccharide (LOS) and a higher-molecular-weight polysaccharide that is believed to form a capsule. The role of these surface polysaccharides in C. jejuni-mediated enteric disease is unclear; however, epitopes associated with the LOS are linked to the development of neurological complications. In Escherichia coli and Salmonella enterica serovar Typhimurium the waaF gene encodes a heptosyltransferase, which catalyzes the transfer of the second L-glycero-D-manno-heptose residue to the core oligosaccharide moiety of lipopolysaccharide (LPS), and mutation of waaF results in a truncated core oligosaccharide. In this report we confirm experimentally that C. jejuni gene Cj1148 encodes the heptosyltransferase II enzyme, WaaF. The Campylobacter waaF gene complements an S. enterica serovar Typhimurium waaF mutation and restores the ability to produce full-sized lipopolysaccharide. To examine the role of WaaF in C. jejuni, waaF mutants were constructed in strains NCTC 11168 and NCTC 11828. Loss of heptosyltransferase activity resulted in the production of a truncated core oligosaccharide, failure to bind specific ligands, and loss of serum reactive GM 1 , asialo-GM 1 , and GM 2 ganglioside epitopes. The mutation of waaF did not affect the higher-molecular-weight polysaccharide supporting the production of a LOS-independent capsular polysaccharide by C. jejuni. The exact structural basis for the truncation of the core oligosaccharide was verified by comparative chemical analysis. The NCTC 11168 core oligosaccharide differs from that known for HS:2 strain CCUG 10936 in possessing an extra terminal disaccharide of galactose-␤(1,3) N-acetylgalactosamine. In comparison, the waaF mutant possessed a truncated molecule consistent with that observed with waaF mutants in other bacterial species.

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Pathogenesis of enteric Campylobacter infection

Cited by 126 publications

References 113 publications

Sulphite : cytochrome c oxidoreductase deficiency in Campylobacter jejuni reduces motility, host cell adherence and invasion

Sulphite : cytochrome c oxidoreductase deficiency in Campylobacter jejuni reduces motility, host cell adherence and invasion

Utilization of Lactoferrin-Bound and Transferrin-Bound Iron by Campylobacter jejuni

Characterization of theCampylobacter jejuniHeptosyltransferase II Gene,waaF, Provides Genetic Evidence that Extracellular Polysaccharide Is Lipid A Core Independent

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