<i>Campylobacter jejuni</i>CsrA Mediates Oxidative Stress Responses, Biofilm Formation, and Host Cell Invasion

Fields, Joshua A.; Thompson, Stuart A.

doi:10.1128/jb.01928-07

Cited by 131 publications

(160 citation statements)

References 70 publications

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“…Recent work in the distantly related C. jejuni is consistent with the B. subtilis model, in which FliW antagonizes CsrA and CsrA inhibits flagellin translation (39). Thus, the noncompetitive mechanism of inhibition that governs the CsrA-FliW-flagellin module is likely to be directly applicable to all FliW-encoding organisms, including members of the firmicutes, the spirochetes, and the deep branches of the proteobacteria (34,39,(45)(46)(47)(48). In contrast, competitive inhibition of CsrA by sRNA has been extensively studied, but only in bacteria belonging to the family of γ-proteobacteria (29).…”

Section: Discussionmentioning

confidence: 49%

“…The phylogenetic distribution of sRNA competitors is poorly understood because of difficulties in predicting sRNA presence, expression, and function, but the conservation of the BarA-UvrY two component system that regulates csrB and csrC expression is largely restricted to the γ-proteobacteria, suggesting the sRNA mechanism of CsrA antagonism is narrowly distributed (34,38,49). Finally we note that, whether an organism uses sRNAs or FliW for regulation, CsrA regulates virulence factors in each pathogen in which it has been studied (1,(45)(46)(47)(48). We suggest that CsrA is a candidate therapeutic target and that the precedent for noncompetitive inhibition can be exploited to isolate noncompetitive inhibitors, which are typically effective at lower doses than competitive counterparts.…”

Section: Discussionmentioning

confidence: 99%

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FliW antagonizes CsrA RNA binding by a noncompetitive allosteric mechanism

Mukherjee

Oshiro

Yakhnin

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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CsrA (carbon storage regulator A) is a widely distributed bacterial RNA binding protein that regulates translation initiation and mRNA stability of target transcripts. In γ-proteobacteria, CsrA activity is competitively antagonized by one or more small RNAs (sRNAs) containing multiple CsrA binding sites, but CsrA in bacteria outside the γ-proteobacteria is antagonized by a protein called FliW. Here we show that FliW of Bacillus subtilis does not bind to the same residues of CsrA required for RNA binding. Instead, CsrA mutants resistant to FliW antagonism (crw) altered residues of CsrA on an allosteric surface of previously unattributed function. Some crw mutants abolished CsrA–FliW binding, but others did not, suggesting that FliW and RNA interaction is not mutually exclusive. We conclude that FliW inhibits CsrA by a noncompetitive mechanism that differs dramatically from the well-established sRNA inhibitors. FliW is highly conserved with CsrA in bacteria, appears to be the ancestral form of CsrA regulation, and represents a widespread noncompetitive mechanism of CsrA control.

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Section: Discussionmentioning

confidence: 49%

Section: Discussionmentioning

confidence: 99%

FliW antagonizes CsrA RNA binding by a noncompetitive allosteric mechanism

Mukherjee

Oshiro

Yakhnin

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…Several bacterial species exhibit altered levels of oxidative stress response proteins depending on the levels of regulation by CsrA (10,29,79). But in B. burgdorferi, overexpression of CsrA Bb does not seem to have an effect on the levels of two critical proteins involved in mediating resistance to oxidative stress, namely, NapA and SodA.…”

Section: Discussionmentioning

confidence: 99%

Overexpression of CsrA (BB0184) Alters the Morphology and Antigen Profiles ofBorrelia burgdorferi

et al. 2009

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“…However, examination of C. jejuni's aggregation and biofilm formation showed no significant difference between the mutants and the wild-type strain (results not shown), indicating that the impaired invasion of the four tlp mutants was not caused by major modifications of global surface structures. We further examined whether the reduced invasion was mediated by altered gene expression of known virulence factors by studying the transcriptional expression of cadF, ciaB, and csrA, encoding a fibronectin binding protein, a host cell internalization protein, and a putative global regulator, respectively (16,26,27). However, Northern blot experiments revealed no change in the expression profiles of cadF, ciaB, and crsA for the invasion-deficient tlp1 and docB mutants (results not shown).…”

Section: Resultsmentioning

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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Campylobacter jejuniCsrA Mediates Oxidative Stress Responses, Biofilm Formation, and Host Cell Invasion

Cited by 131 publications

References 70 publications

FliW antagonizes CsrA RNA binding by a noncompetitive allosteric mechanism

FliW antagonizes CsrA RNA binding by a noncompetitive allosteric mechanism

Overexpression of CsrA (BB0184) Alters the Morphology and Antigen Profiles ofBorrelia burgdorferi

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

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