CapC, a Novel Autotransporter and Virulence Factor of Campylobacter jejuni.

is recognized as an important causative agent of bacterial gastroenteritis in the developed world. Despite the identification of several factors contributing to infection, characterization of the virulence strategies employed by remains a significant challenge. Bacterial autotransporter proteins are a major class of secretory proteins in Gram-negative bacteria, and notably, many autotransporter proteins contribute to bacterial virulence.

Growth of Campylobacter jejuni on nitrate and nitrite: electron transport to NapA and NrfA via NrfH and distinct roles for NrfA and the globin Cgb in protection against nitrosative stress.

Pathways of electron transport to periplasmic nitrate (NapA) and nitrite (NrfA) reductases have been investigated in Campylobacter jejuni, a microaerophilic food-borne pathogen. The nap operon is unusual in lacking napC (encoding a tetra-haem c-type cytochrome) and napF, but contains a novel gene of unknown function, napL. The iron-sulphur protein NapG has a major role in electron transfer to the NapAB complex, but we show that slow nitrate-dependent growth of a napG mutant can be sustained by electron transfer from NrfH, the electron donor to the nitrite reductase NrfA.

Oxygen reactivity of both respiratory oxidases in Campylobacter jejuni: the cydAB genes encode a cyanide-resistant, low-affinity oxidase that is not of the cytochrome bd type.

The microaerophilic bacterium Campylobacter jejuni is a significant food-borne pathogen and is predicted to possess two terminal respiratory oxidases with unknown properties. Inspection of the genome reveals an operon (cydAB) apparently encoding a cytochrome bd-like oxidase homologous to oxidases in Escherichia coli and Azotobacter vinelandii. However, C.

Purification and spectroscopic characterization of Ctb, a group III truncated hemoglobin implicated in oxygen metabolism in the food-borne pathogen Campylobacter jejuni.

Campylobacter jejuni is a food-borne bacterial pathogen that possesses two distinct hemoglobins, encoded by the ctb and cgb genes. The former codes for a truncated hemoglobin (Ctb) in group III, an assemblage of uncharacterized globins in diverse clinically and technologically significant bacteria. Here, we show that Ctb purifies as a monomeric, predominantly oxygenated species.

A truncated haemoglobin implicated in oxygen metabolism by the microaerophilic food-borne pathogen Campylobacter jejuni.

Of the three groups of haemoglobins identified in micro-organisms (single-domain globins, flavohaemoglobins and truncated globins), the last group is the least well understood. The function of the truncated haemoglobin (Ctb) encoded by Cj0465c in the microaerophilic food-borne bacterial pathogen Campylobacter jejuni was investigated by constructing a ctb mutant and characterizing its phenotype. The effects of the ctb mutation on the kinetics of terminal oxidase function in C.

NssR, a member of the Crp-Fnr superfamily from Campylobacter jejuni, regulates a nitrosative stress-responsive regulon that includes both a single-domain and a truncated haemoglobin.

Consistent with its role as a nitric oxide (NO)-detoxifying globin in Campylobacter jejuni, Cgb (Campylobacter globin) expression is strongly and specifically induced following exposure to nitrosative stress, suggesting a previously unrecognized capacity for NO-related stress sensing in this food-borne pathogen. In this study, Fur and PerR have been eliminated as major regulators of cgb, and NssR (Cj0466), a member of the Crp-Fnr superfamily, has been identified as the major positive regulatory factor that controls nitrosative stress-responsive expression of this gene. Accordingly, disruption of nssR resulted in the abolition of inducible cgb expression, which was restored by a complementing chromosomal insertion of the wild-type gene with its indigenous promoter at a second location.

Role of an inducible single-domain hemoglobin in mediating resistance to nitric oxide and nitrosative stress in Campylobacter jejuni and Campylobacter coli.

Campylobacter jejuni expresses two hemoglobins, each of which exhibits a heme pocket and structural signatures in common with vertebrate and plant globins. One of these, designated Cgb, is homologous to Vgb from Vitreoscilla stercoraria and does not possess the reductase domain seen in the flavohemoglobins. A Cgb-deficient mutant of C.

Detection and enumeration of Campylobacter jejuni and Campylobacter coli by indirect impedimetry with an oxygen scavenging system.

Six strains of Campylobacter jejuni and Campylobacter coli were shown to grow in a variety of media, but, with one exception, they were unable to produce sufficient change in the electrical properties of the medium to allow their detection by impedance monitoring. With the use of an indirect method based on absorption of evolved carbon dioxide and a medium containing the oxygen scavenger Oxyrase, all strains were detectable, and correlations between time to detection and the logarithm of the inoculum level were excellent. The level of interstrain variation was sufficiently low that all data could be consolidated into a single calibration curve (r = 0.

The role of iron in Campylobacter gene regulation, metabolism and oxidative stress defense.

Enteric Campylobacter species cause gastrointestinal diseases in humans. Like almost all organisms, campylobacters have an absolute requirement for iron, but are faced with variable availability of iron in the environment and host tissues. Campylobacters have developed mechanisms to scavenge sufficient iron for metabolism and growth.

Quorum sensing in Campylobacter jejuni: detection of a luxS encoded signalling molecule.

The expression of a wide variety of physiological functions in many bacterial species is modulated by quorum sensing, a population-dependent signalling mechanism that involves the production and detection of extracellular signalling molecules. The genome sequence of Campylobacter jejuni NCTC 11168 contains a gene encoding an orthologue of LuxS, which is required for autoinducer-2 (AI-2) production in other bacterial species, but does not contain genes predicted to encode any known acyl-homoserine lactone synthetase. This study demonstrates that C.

The physiology of Campylobacter species and its relevance to their role as foodborne pathogens.

Campylobacter jejuni and C. coli are recognised as the leading causes of bacterial foodborne diarrhoeal disease throughout the development world. While most foodborne bacterial pathogens are considered to be relatively robust organisms, as a consequence of the necessity to survive the inimical conditions imposed by food processing and preservation, Campylobacter species have uniquely fastidious growth requirements and an unusual sensitivity to environmental stress.

Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange.

A gene encoding catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.