Association with HeLa cells of Campylobacter jejuni and Campylobacter coli isolated from human feces

Fauchère, J.L.; Rosenau, Agnès; Véron, Michel; Moyen, E.; Richard, S.; Pfister, A

doi:10.1128/iai.54.2.283-287.1986

Cited by 110 publications

(48 citation statements)

References 28 publications

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“…As in the case of other intestinal pathogens, the ability of C. jejuni to colonize the gastrointestinal tract by binding to epithelial or other cells has been proposed to be essential for disease production. Fauchere et al (1986) found that C. jejuni isolated from individuals with fever and diarrhoea exhibited greater binding to epithelial cells than strains isolated from individuals without diarrhoea or fever. Studies have been performed to identify and characterize potential Campylobacter adhesins that mediate the organism's attachment to host cells.…”

Section: Introductionmentioning

confidence: 88%

Identification and molecular cloning of a gene encoding a fibronectin‐binding protein (CadF) from Campylobacter jejuni

Konkel

Garvis

Tipton

et al. 1997

Molecular Microbiology

288

238

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SummaryCampylobacter jejuni, a Gram-negative bacterium, is a common cause of gastrointestinal disease. By analogy with other enteric pathogens such as Salmonella and Shigella, the ability of C. jejuni to bind to host cells is thought to be essential in the pathogenesis of enteritis. Scanning electron microscopy of infected INT407 cells suggested that C. jejuni bound to a component of the extracellular matrix. Binding assays using immobilized extracellular matrix proteins and soluble fibronectin showed specific and saturable binding of fibronectin to C. jejuni. Ligand immunoblot assays using 125 I-labelled fibronectin revealed specific binding to an outer membrane protein with an apparent molecular mass of 37 kDa. A rabbit antiserum, raised against the gel-purified protein, reacted with a 37 kDa protein in all C. jejuni isolates (n ¼ 15) as tested by immunoblot analysis. Antibodies present in convalescent serum from C. jejuni-infected individuals also recognized a 37 kDa protein. The gene encoding the immunoreactive 37 kDa protein was cloned and sequenced. Sequencing of overlapping DNA fragments revealed an open reading frame (ORF) that encodes a protein of 326 amino acids with a calculated molecular mass of 36 872 Da. The deduced amino acid sequence of the ORF exhibited 52% similarity and 28% identity to the root adhesin protein from Pseudomonas fluorescens. Isogenic C. jejuni mutants which lack the 37 kDa outer membrane protein, which we have termed CadF, displayed significantly reduced binding to fibronectin. Biotinylated fibronectin bound to a protein with an apparent molecular mass of 37 kDa in the outer membrane protein extracts from wild-type C. jejuni as judged by ligandbinding blots. These results indicate that the binding of C. jejuni to fibronectin is mediated by the 37 kDa outer membrane protein which is conserved among C. jejuni isolates.

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Section: Introductionmentioning

confidence: 88%

Identification and molecular cloning of a gene encoding a fibronectin‐binding protein (CadF) from Campylobacter jejuni

Konkel

Garvis

Tipton

et al. 1997

Molecular Microbiology

288

238

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“…Adhesion to intestinal epithelial cells and their invasion are important for C. jejuni pathogenicity (Fauchere et al, 1986;Black et al, 1988;De Melo et al, 1989;Konkel et al, 1992), and CPS is thought to be essential for these processes (Bacon et al, 2001;Bachtiar et al, 2007). We therefore assessed our mutants for adhesion and invasion with Caco-2 intestinal epithelial cells.…”

Section: The Heptose Modification Pathway Is Important For Invasion Omentioning

confidence: 99%

“…Flagella-mediated motility also contributes to the virulence of C. jejuni (Biswas et al, 2007), as it facilitates colonization of the mucus layer covering the intestinal epithelium (Lee et al, 1986;Beery et al, 1988) and subsequent invasion of epithelial cells (Pei and Blaser, 1993;Jin et al, 2001;Konkel et al, 2005;Vijayakumar et al, 2006). Survival of C. jejuni within macrophages for several days is also a key virulence factor (Kiehlbauch et al, 1985;Day et al, 2000), and epithelial and macrophage cell damage resulting from invasion may be critical for the inflammatory response elicited by C. jejuni infection (Manninen et al, 1982;Newell and Pearson, 1984;Newell et al, 1985;Fauchere et al, 1986;Szymanski et al, 1995;Biswas et al, 2000). Further, the surface expression of lipooligosaccharide (LOS), which in many C. jejuni strains mimics human gangliosides, has been associated with autoimmune reactions implicated in the Guillain-Barre and Miller Fischer syndromes (Mishu and Blaser, 1993;Yuki et al, 1994;Salloway et al, 1996;Godschalk et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Role of capsular modified heptose in the virulence of Campylobacter jejuni

Wong

Lange

Houle³

et al. 2015

Molecular Microbiology

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SummaryThe Campylobacter jejuni capsular polysaccharide is important for virulence and often contains a modified heptose. In strain ATCC 700819 (a.k.a. NCTC 11168), the modified heptose branches off from the capsular backbone and is directly exposed to the environment. We reported previously that the enzymes encoded by wcaG, mlghB and mlghC are involved in heptose modification. Here, we show that inactivation of any of these genes leads to production of capsule lacking modified heptose and alters the transcription of other capsule modification genes differentially. Inactivation of mlghB or mlghC, but not of wcaG, decreased susceptibility to bile salts and abrogated invasion of intestinal cells. All mutants showed increased sensitivity to serum killing, especially wcaG::cat, and had defects in colonization and persistence in chicken intestine, but did not show significant differences in adhesion, phagocytosis and intracellular survival in murine macrophages. Together, our findings suggest that the capsular heptose modification pathway contributes to bacterial resistance against gastrointestinal host defenses and supports bacterial persistence via its role in serum resistance and invasion of intestinal cells. Our data further suggest a dynamic regulation of expression of this pathway in the gastrointestinal tract.

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“…Following adherence, host-cell invasion and toxin production appear to contribute to C. jejuni pathogenesis and subsequent host cell tissue necrosis (Everest et al ., 1992;Konkel and Cieplak, 1992;Konkel et al ., 1993;Russell et al ., 1993;Wassenaar, 1997;Pickett and Whitehouse, 1999). Fauchère et al . (1986) found that C. jejuni isolates from individuals with fever and diarrhoea adhered to cultured cells at a greater efficiency than those isolates recovered from asymptomatic individuals.…”

Section: Introductionmentioning

confidence: 99%

Identification of a fibronectin‐binding domain within the Campylobacter jejuni CadF protein

Konkel

Christensen

Keech

et al. 2005

Molecular Microbiology

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Association with HeLa cells of Campylobacter jejuni and Campylobacter coli isolated from human feces

Cited by 110 publications

References 28 publications

Identification and molecular cloning of a gene encoding a fibronectin‐binding protein (CadF) from Campylobacter jejuni

Identification and molecular cloning of a gene encoding a fibronectin‐binding protein (CadF) from Campylobacter jejuni

Role of capsular modified heptose in the virulence of Campylobacter jejuni

Identification of a fibronectin‐binding domain within the Campylobacter jejuni CadF protein

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