Differentiated Caco-2 cells as a model for enteric invasion by Campylobacter jejuni and C. coli

Everest, Paul; Goossens, Herman; Butzler, Jean‐Paul; Lloyd, D. R.; Knutton, Stuart; Ketley, Julian M.; Williams, Peter H.

doi:10.1099/00222615-37-5-319

Cited by 154 publications

(130 citation statements)

References 25 publications

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“…The data shown are the means of triplicate experiments. 13,15,20). In this study, kinetic analysis of C. jejuni invasion into INT-407 cells revealed that optimal invasion efficiency (percentage of the inoculum recovered as internalized at the end of the gentamicin treatment assay) was highest at the lowest MOI of 1 but that a maximal number of internalized C. jejuni was detected at 100 MOI.…”

Section: Discussionmentioning

confidence: 98%

Infection with Campylobacter jejuni Induces Tyrosine‐Phosphorylated Proteins into INT‐407 Cells

Biswas

Niwa

Itoh

2004

Microbiology and Immunology

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The mechanisms used by Campylobacter jejuni to induce internalization into host intestinal epithelial cells have not been defined. In this study, we obtained evidence that exposure of INT‐407 cells to protein kinase inhibitors results in decreased invasion of these cells by C. jejuni in a dose dependent manner. Preincubation of INT‐407 cells in the presence of staurosporine, tyrphostin 46 and genistein decreased invasion of these cells by C. jejuni significantly. Moreover, C. jejuni infection of INT‐407 cells induced tyrosine phosphorylation of several Triton X‐100 soluble proteins with approximate molecular weights of 170, 145, 90, 60 and 55 kDa that were absent or reduced in the presence of genistein in cells after 1 hr of pretreatment. These data suggest that tyrosine protein kinase‐linked pathways strongly regulate the internalization of C. jejuni into intestinal epithelial cells.

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Section: Discussionmentioning

confidence: 98%

Infection with Campylobacter jejuni Induces Tyrosine‐Phosphorylated Proteins into INT‐407 Cells

Biswas

Niwa

Itoh

2004

Microbiology and Immunology

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“…Quantitation data are summarized in Table 2. (B) To ensure equal amounts of bacteria in each sample, the corresponding bacterial pellets were probed with α-HtrA antibodies [35][36][37][38]. We are interested in characterizing bacterial and host factors involved in C. jejuni transmigration.…”

Section: Discussionmentioning

confidence: 99%

Extracellular secretion of protease HtrA fromCampylobacter jejuniis highly efficient and independent of its protease activity and flagellum

Boehm¹,

Haenel²,

Hoy³

et al. 2013

European Journal of Microbiology and Immunology

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The serine protease HtrA of C. jejuni has been identified as a novel secreted virulence factor which opens cell-to-cell junctions by cleaving E-cadherin. Efficient C. jejuni transmigration across polarized human epithelial cells requires the intact flagellum and HtrA; however, the mechanism of HtrA secretion into the supernatant is unknown. Here we show that HtrA secretion is highly efficient and does not require its proteolytic activity because the protease-inactive S197A mutant is secreted like wild-type HtrA. In addition, the flagellar mutants ΔflaA/B, ΔfliI, ΔflgH, ΔflhA, ΔflhB, and ΔflgS were also able to secrete HtrA in high amounts, while they were strongly attenuated in secreting the well-known invasion antigen CiaB. We also tested several culture media and cell lines of different origin such as human, mouse, hamster, dog, and chicken for their ability to influence HtrA secretion. Interestingly, HtrA was effectively secreted in the presence of most but not all cell lines and media, albeit at different levels, but secretion was significantly higher when fetal calf serum (FCS) was added. These results demonstrate that HtrA secretion by Campylobacter proceeds independent of HtrA's protease activity, the flagellum and origin of cell lines, but can be strongly enhanced by molecular compound(s) present in FCS.

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“…Cells were cultivated in RPMI 1640 supplemented with 10% fetal bovine serum and 0.02% each penicillin and streptomycin at 37°C in 5% CO 2 . Bacterial invasion was determined by using a gentamicin protection assay (14). Briefly, cells were grown to approximately 80% confluence in 12-well tissue culture plates, and after three washes with Hanks balanced salt solution, the cells were infected with C. jejuni at a …”

Section: Methodsmentioning

confidence: 99%

Energy Taxis Drives Campylobacter jejuni toward the Most Favorable Conditions for Growth

Vegge

Brøndsted

et al. 2009

Appl Environ Microbiol

121

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Campylobacter jejuni is a serious food-borne bacterial pathogen in the developed world. Poultry is a major reservoir, and C. jejuni appears highly adapted to the gastrointestinal tract of birds. Several factors are important for chicken colonization and virulence, including a taxis mechanism for environmental navigation. To explore the mechanism of chemotaxis in C. jejuni, we constructed mutants with deletions of five putative mcp (methyl-accepting chemotaxis protein) genes (tlp1, tlp2, tlp3, docB, and docC). Surprisingly, the deletions did not affect the chemotactic behavior of the mutants compared to that of the parental strain. However, the tlp1, tlp3, docB, and docC mutant strains displayed a 10-fold decrease in the ability to invade human epithelial and chicken embryo cells, hence demonstrating that the corresponding proteins affect the host interaction. LAsparagine, formate, D-lactate, and chicken mucus were identified as new attractants of C. jejuni, and we observed that chemical substances promoting tactic attraction are all known to support the growth of this organism. The attractants could be categorized as carbon sources and electron donors and acceptors, and we furthermore observed a correlation between an attractant's potency and its efficiency as an energy source. The tactic attraction was inhibited by the respiratory inhibitors HQNO (2-n-heptyl-4-hydroxyquinoline N-oxide) and sodium azide, which significantly reduce energy production by oxidative phosphorylation. These findings strongly indicate that energy taxis is the primary force in environmental navigation by C. jejuni and that this mechanism drives the organism toward the optimal chemical conditions for energy generation and colonization.

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Differentiated Caco-2 cells as a model for enteric invasion by Campylobacter jejuni and C. coli

Cited by 154 publications

References 25 publications

Infection with Campylobacter jejuni Induces Tyrosine‐Phosphorylated Proteins into INT‐407 Cells

Infection with Campylobacter jejuni Induces Tyrosine‐Phosphorylated Proteins into INT‐407 Cells

Extracellular secretion of protease HtrA fromCampylobacter jejuniis highly efficient and independent of its protease activity and flagellum

Energy Taxis Drives Campylobacter jejuni toward the Most Favorable Conditions for Growth

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