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Molecular mechanisms and biological role of Campylobacter jejuni attachment to host cells.

ABSTRACT: Adhesion to host cells is an important step in pathogenesis of Campylobacter jejuni, which is the most prevalent bacterial cause of human gastroenteritis worldwide. In contrast to other bacteria such as E. coli and Salmonella, adherence of C. jejuni is not mediated by fimbria or pili. A number of C. jejuni adhesion-related factors have been described. However, the results obtained by different researchers in different laboratories are often contradictory and inconclusive, with only some of the factors described being confirmed as true adhesins. In this review, we present the current state of studies on the mechanisms of attachment of C. jejuni to host cells.

SUBMITTER: Rubinchik S

PROVIDER: S-EPMC3933988 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

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Molecular mechanisms and biological role of Campylobacter jejuni attachment to host cells.

Rubinchik S S Seddon A A Karlyshev A V AV

European journal of microbiology & immunology 20120317 1

Adhesion to host cells is an important step in pathogenesis of Campylobacter jejuni, which is the most prevalent bacterial cause of human gastroenteritis worldwide. In contrast to other bacteria such as E. coli and Salmonella, adherence of C. jejuni is not mediated by fimbria or pili. A number of C. jejuni adhesion-related factors have been described. However, the results obtained by different researchers in different laboratories are often contradictory and inconclusive, with only some of the f ...[more]

PMID: 24611119

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Project description:BackgroundMacrolide is the drug of choice to treat human campylobacteriosis, but Campylobacter resistance to this antibiotic is rising. The mechanisms employed by Campylobacter jejuni to adapt to erythromycin treatment remain unknown and are examined in this study. The transcriptomic response of C. jejuni NCTC 11168 to erythromycin (Ery) treatment was determined by competitive microarray hybridizations. Representative genes identified to be differentially expressed were further characterized by constructing mutants and assessing their involvement in antimicrobial susceptibility, oxidative stress tolerance, and chicken colonization.ResultsFollowing the treatment with an inhibitory dose of Ery, 139 genes were up-regulated and 119 were down-regulated. Many genes associated with flagellar biosynthesis and motility was up-regulated, while many genes involved in tricarboxylic acid cycle, electron transport, and ribonucleotide biosynthesis were down-regulated. Exposure to a sub-inhibitory dose of Ery resulted in differential expression of much fewer genes. Interestingly, two putative drug efflux operons (cj0309c-cj0310c and cj1173-cj1174) were up-regulated. Although mutation of the two operons did not alter the susceptibility of C. jejuni to antimicrobials, it reduced Campylobacter growth under high-level oxygen. Another notable finding is the consistent up-regulation of cj1169c-cj1170c, of which cj1170c encodes a known phosphokinase, an important regulatory protein in C. jejuni. Mutation of the cj1169c-cj1170c rendered C. jejuni less tolerant to atmospheric oxygen and reduced Campylobacter colonization and transmission in chickens.ConclusionsThese findings indicate that Ery treatment elicits a range of changes in C. jejuni transcriptome and affects the expression of genes important for in vitro and in vivo adaptation. Up-regulation of motility and down-regulation of energy metabolism likely facilitate Campylobacter to survive during Ery treatment. These findings provide new insight into Campylobacter adaptive response to antibiotic treatment and may help to understand the mechanisms underlying antibiotic resistance development.

Project description:Campylobacter jejuni is a major cause of bacterial foodborne illness in humans worldwide. Bacterial entry into a host eukaryotic cell involves the initial steps of adherence and invasion, which generally activate several cell-signaling pathways that induce the activation of innate defense systems, which leads to the release of proinflammatory cytokines and induction of apoptosis. Recent studies have reported that the unfolded protein response (UPR), a system to clear unfolded proteins from the endoplasmic reticulum (ER), also participates in the activation of cellular defense mechanisms in response to bacterial infection. However, no study has yet investigated the role of UPR in C. jejuni infection. Hence, the aim of this study was to deduce the role of UPR signaling via induction of ER stress in the process of C. jejuni infection. The results suggest that C. jejuni infection suppresses global protein translation. Also, 12 h of C. jejuni infection induced activation of the eIF2α pathway and expression of the transcription factor CHOP. Interestingly, bacterial invasion was facilitated by knockdown of UPR-associated signaling factors and treatment with the ER stress inducers, thapsigargin and tunicamycin, decreased the invasive ability of C. jejuni. An investigation into the mechanism of UPR-mediated inhibition of C. jejuni invasion showed that UPR signaling did not affect bacterial adhesion to or survival in the host cells. Further, Salmonella Enteritidis or FITC-dextran intake were not regulated by UPR signaling. These results indicated that the effect of UPR on intracellular intake was specifically found in C. jejuni infection. These findings are the first to describe the role of UPR in C. jejuni infection and revealed the participation of a new signaling pathway in C. jejuni invasion. UPR signaling is involved in defense against the early step of C. jejuni invasion and thus presents a potential therapeutic target for the treatment of C. jejuni infection.

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Molecular mechanisms and biological role of Campylobacter jejuni attachment to host cells.

Publications

Molecular mechanisms and biological role of Campylobacter jejuni attachment to host cells.

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