The role of respiratory donor enzymes in Campylobacter jejuni host colonization and physiology

Weerakoon, Dilan R.; Borden, Nathan J.; Goodson, Carrie; Grimes, J. L.; Olson, Jonathan W.

doi:10.1016/j.micpath.2009.04.009

Cited by 70 publications

(109 citation statements)

References 33 publications

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“…Formate dehydrogenase serves as an electron donor enzyme by the oxidation of formate to CO 2 , protons and electrons. The released electrons, in turn, enter the electron transport chain to contribute to the proton ion gradient (Weerakoon et al, 2009). The discovery that Cj0952c-Cj0951c mediates the chemotaxis of C. jejuni in the presence of formic acid raised the question of whether the particular composition of this receptor in the clinical isolate B2 is related to the utilization of formic acid by formate dehydrogenase.…”

Section: Discussionmentioning

confidence: 99%

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

et al. 2010

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Campylobacter jejuni, an important food-borne bacterial pathogen in industrialized countries and in the developing world, is one of the major causes of bacterial diarrhoea. To identify genes which are important for the invasion of host cells by the pathogen, we screened altogether 660 clones of a transposon-generated mutant library based on the clinical C. jejuni isolate B2. Thereby, we identified a clone with a transposon insertion in gene cj0952c. As in the well-characterized C. jejuni strain NCTC 11168, the corresponding protein together with the gene product of the adjacent gene cj0951c consists of two transmembrane domains, a HAMP domain and a putative MCP domain, which together are thought to act as a chemoreceptor, designated Tlp7. In this report we show that genes cj0952c and cj0951c (i) are important for the host cell invasion of the pathogen, (ii) are not translated as one protein in C. jejuni isolate B2, contradicting the idea of a postulated read-through mechanism, (iii) affect the motility of C. jejuni, (iv) alter the chemotactic behaviour of the pathogen towards formic acid, and (v) are not related to the utilization of formic acid by formate dehydrogenase.

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Section: Discussionmentioning

confidence: 99%

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

et al. 2010

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Section: Introductionmentioning

confidence: 97%

“…Nevertheless, a hydB null mutant shows only a modest decrease in colonization of the caecum of chicks, similar to a formate dehydrogenase (fdhA) null mutant (Weerakoon et al, 2009). Significantly, however, colonization by a hydB/fdhA double mutant is severely impaired (Weerakoon et al, 2009). Together, these data suggest that the absence of hydrogenase is compensated for by the presence of Fdh and vice versa in the single mutants of C. jejuni, indicating the importance of both hydrogen and formate as electron donors in the chick caecum.…”

Section: Introductionmentioning

confidence: 99%

“…The C. jejuni NCTC 11168 genome encodes an energyconserving membrane-bound NiFe-type uptake hydrogenase (HydABCD, Cj1267-1264 (Hoffman & Goodman, 1982;Parkhill et al, 2000;Weerakoon et al, 2009), the HydAB subunits of which are targeted to the periplasm by the twin arginine translocase (Tat) system (Hitchcock et al, 2010). C. jejuni hydA (cj1267c) encodes the small subunit Fe-S protein, which contains an N-terminal Tat motif; hydB (cj1266c) encodes the NiFe active site containing the large subunit; hydC (cj1265c) encodes a membrane-anchored b-type cytochrome; and hydD (cj1264c) encodes a protease involved in enzyme maturation (Vignais et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

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Hydrogenase activity in the foodborne pathogen Campylobacter jejuni depends upon a novel ABC-type nickel transporter (NikZYXWV) and is SlyD-independent

et al. 2012

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Campylobacter jejuni is a human pathogen of worldwide significance. It is commensal in the gut of many birds and mammals, where hydrogen is a readily available electron donor. The bacterium possesses a single membrane-bound, periplasmic-facing NiFe uptake hydrogenase that depends on the acquisition of environmental nickel for activity. The periplasmic binding protein Cj1584 (NikZ) of the ATP binding cassette (ABC) transporter encoded by the cj1584c-cj1580c (nikZYXWV) operon in C. jejuni strain NCTC 11168 was found to be nickel-repressed and to bind free nickel ions with a submicromolar K d value, as measured by fluorescence spectroscopy. Unlike the Escherichia coli NikA protein, NikZ did not bind EDTA-chelated nickel and lacks key conserved residues implicated in metallophore interaction. A C. jejuni cj1584c null mutant strain showed an approximately 22-fold decrease in intracellular nickel content compared with the wildtype strain and a decreased rate of uptake of 63 NiCl 2 . The inhibition of residual nickel uptake at higher nickel concentrations in this mutant by hexa-ammine cobalt (III) chloride or magnesium ions suggests that low-affinity uptake occurs partly through the CorA magnesium transporter. Hydrogenase activity was completely abolished in the cj1584c mutant after growth in unsupplemented media, but was fully restored after growth with 0.5 mM nickel chloride. Mutation of the putative metallochaperone gene slyD (cj0115) had no effect on either intracellular nickel accumulation or hydrogenase activity. Our data reveal a strict dependence of hydrogenase activity in C. jejuni on high-affinity nickel uptake through an ABC transporter that has distinct properties compared with the E. coli Nik system.

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“…Electrons liberated from formate by FdhA in the periplasm are passed to the iron/sulfur-containing protein FdhB and then to the cytochrome b-containing FdhC subunit; FdhD is also required for FDH activity, but its precise role is not known. Analyses of C. jejuni fdhA and fdhD mutants have implicated a role for FDH in chick colonization, survival at a low pH, and the induction of pathogenesis in a gnotobiotic mouse disease model (6,14,63,81).…”

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confidence: 99%

FdhTU-Modulated Formate Dehydrogenase Expression and Electron Donor Availability Enhance Recovery ofCampylobacter jejunifollowing Host Cell Infection

et al. 2012

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bCampylobacter jejuni is a food-borne bacterial pathogen that colonizes the intestinal tract and causes severe gastroenteritis. Interaction with host epithelial cells is thought to enhance severity of disease, and the ability of C. jejuni to modulate its metabolism in different in vivo and environmental niches contributes to its success as a pathogen. A C. jejuni operon comprising two genes that we designated fdhT (CJJ81176_1492) and fdhU (CJJ81176_1493) is conserved in many bacterial species. Deletion of fdhT or fdhU in C. jejuni resulted in apparent defects in adherence and/or invasion of Caco-2 epithelial cells when assessed by CFU enumeration on standard Mueller-Hinton agar. However, fluorescence microscopy indicated that each mutant invaded cells at wild-type levels, instead suggesting roles for FdhTU in either intracellular survival or postinvasion recovery. The loss of fdhU caused reduced mRNA levels of formate dehydrogenase (FDH) genes and a severe defect in FDH activity. Cell infection phenotypes of a mutant deleted for the FdhA subunit of FDH and an ⌬fdhU ⌬fdhA double mutant were similar to those of a ⌬fdhU mutant, which likewise suggested that FdhU and FdhA function in the same pathway. Cell infection assays followed by CFU enumeration on plates supplemented with sodium sulfite abolished the ⌬fdhU and ⌬fdhA mutant defects and resulted in significantly enhanced recovery of all strains, including wild type, at the invasion and intracellular survival time points. Collectively, our data indicate that FdhTU and FDH are required for optimal recovery following cell infection and suggest that C. jejuni alters its metabolic potential in the intracellular environment.

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The role of respiratory donor enzymes in Campylobacter jejuni host colonization and physiology

Cited by 70 publications

References 33 publications

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

Hydrogenase activity in the foodborne pathogen Campylobacter jejuni depends upon a novel ABC-type nickel transporter (NikZYXWV) and is SlyD-independent

FdhTU-Modulated Formate Dehydrogenase Expression and Electron Donor Availability Enhance Recovery ofCampylobacter jejunifollowing Host Cell Infection

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