Characterization of Two Putative Cytochrome
            <i>c</i>
            Peroxidases of
            <i>Campylobacter jejuni</i>
            Involved in Promoting Commensal Colonization of Poultry

Bingham-Ramos, Lacey K.; Hendrixson, David R.

doi:10.1128/iai.01430-07

Cited by 55 publications

(49 citation statements)

References 33 publications

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“…Recovery of wholecell lysates and fraction of C. jejuni strains into subcellular compartments for analysis of localization of proteins from the inner membrane, outer membrane, periplasm, and cytoplasm were performed as previously described (65). Proteins from each fraction representing equivalent cell numbers (∼200 μL of a C. jejuni culture at an OD 600 0.8) were loaded onto 10% SDS/PAGE gels and then were transferred to membranes for immunoblot analysis.…”

Section: Methodsmentioning

confidence: 99%

Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold

Beeby

Ribardo

Brennan

et al. 2016

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

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186

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Although it is known that diverse bacterial flagellar motors produce different torques, the mechanism underlying torque variation is unknown. To understand this difference better, we combined genetic analyses with electron cryo-tomography subtomogram averaging to determine in situ structures of flagellar motors that produce different torques, from Campylobacter and Vibrio species. For the first time, to our knowledge, our results unambiguously locate the torque-generating stator complexes and show that diverse high-torque motors use variants of an ancestrally related family of structures to scaffold incorporation of additional stator complexes at wider radii from the axial driveshaft than in the model enteric motor. We identify the protein components of these additional scaffold structures and elucidate their sequential assembly, demonstrating that they are required for stator-complex incorporation. These proteins are widespread, suggesting that different bacteria have tailored torques to specific environments by scaffolding alternative stator placement and number. Our results quantitatively account for different motor torques, complete the assignment of the locations of the major flagellar components, and provide crucial constraints for understanding mechanisms of torque generation and the evolution of multiprotein complexes.

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Section: Methodsmentioning

confidence: 99%

Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold

Beeby

Ribardo

Brennan

et al. 2016

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

Self Cite

186

262

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“…C. jejuni NCTC11168 contains one catalase (KatA), two cytochrome c peroxidases (Cj0358 and Cj0020c), and three peroxiredoxins (AhpC, Tpx, and Bcp) (34). KatA, Tpx, and Bcp have been shown to contribute, at least to some extent, to H 2 O 2 detoxification in C. jejuni (5,17), and Cj0358 and Cj0020c have been demonstrated to have peroxidase activity (11). AhpC has also been demonstrated to scavenge H 2 O 2 in E. coli (39) and likely performs a similar function in C. jejuni.…”

Section: Discussionmentioning

confidence: 99%

Cj1386 Is an Ankyrin-Containing Protein Involved in Heme Trafficking to Catalase in Campylobacter jejuni

2012

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Campylobacter jejuni, a microaerophilic bacterium, is the most frequent cause of human bacterial gastroenteritis. C. jejuni is exposed to harmful reactive oxygen species (ROS) produced during its own normal metabolic processes and during infection from the host immune system and from host intestinal microbiota. These ROS will damage DNA and proteins and cause peroxidation of lipids. Consequently, identifying ROS defense mechanisms is important for understanding how Campylobacter survives this environmental stress during infection. Construction of a ⌬Cj1386 isogenic deletion mutant and phenotypic assays led to its discovery as a novel oxidative stress defense gene. The ⌬Cj1386 mutant has an increased sensitivity toward hydrogen peroxide. The Cj1386 gene is located directly downstream from katA (catalase) in the C. jejuni genome. A ⌬katA⌬ Cj1386 double deletion mutant was constructed and exhibited a sensitivity to hydrogen peroxide similar to that seen in the ⌬Cj1386 and ⌬katA single deletion mutants. This observation suggests that Cj1386 may be involved in the same detoxification pathway as catalase. Despite identical KatA abundances, catalase activity assays showed that the ⌬Cj1386 mutant had a reduced catalase activity relative to that of wild-type C. jejuni. Heme quantification of KatA protein from the ⌬Cj1386 mutant revealed a significant decrease in heme concentration. This indicates an important role for Cj1386 in heme trafficking to KatA within C. jejuni. Interestingly, the ⌬Cj1386 mutant had a reduced ability to colonize the ceca of chicks and was outcompeted by the wild-type strain for colonization of the gastrointestinal tract of neonate piglets. These results indicate an important role for Cj1386 in Campylobacter colonization and pathogenesis.

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“…This study identified 29 mutants with reduced colonization capacities and provided a foundation for more in-depth studies into potential colonization factors of C. jejuni. From this study and subsequent studies, a better understanding of C. jejuni cytochrome c peroxidases and glycosylated proteins that are involved in commensal colonization has been acquired (5,20,21).…”

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confidence: 99%

Analysis of the LIV System of Campylobacter jejuni Reveals Alternative Roles for LivJ and LivK in Commensalism beyond Branched-Chain Amino Acid Transport

Ribardo

Hendrixson

2011

J Bacteriol

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Campylobacter jejuni is a leading cause of diarrheal disease in humans and an intestinal commensal in poultry and other agriculturally important animals. These zoonotic infections result in significant amounts of C. jejuni present in the food supply to contribute to disease in humans. We previously found that a transposon insertion in Cjj81176_1038, encoding a homolog of the Escherichia coli LivJ periplasmic binding protein of the leucine, isoleucine, and valine (LIV) branched-chain amino acid transport system, reduced the commensal colonization capacity of C. jejuni 81-176 in chicks. Cjj81176_1038 is the first gene of a six-gene locus that encodes homologous components of the E. coli LIV system. By analyzing mutants with in-frame deletions of individual genes or pairs of genes, we found that this system constitutes a LIV transport system in C. jejuni responsible for a high level of leucine acquisition and, to a lesser extent, isoleucine and valine acquisition. Despite each LIV protein being required for branched-chain amino acid transport, only the LivJ and LivK periplasmic binding proteins were required for wild-type levels of commensal colonization of chicks. All LIV permease and ATPase components were dispensable for in vivo growth. These results suggest that the biological functions of LivJ and LivK for colonization are more complex than previously hypothesized and extend beyond a role for binding and acquiring branched-chain amino acids during commensalism. In contrast to other studies indicating a requirement and utilization of other specific amino acids for colonization, acquisition of branched-chain amino acids does not appear to be a determinant for C. jejuni during commensalism.

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Characterization of Two Putative Cytochrome c Peroxidases of Campylobacter jejuni Involved in Promoting Commensal Colonization of Poultry

Cited by 55 publications

References 33 publications

Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold

Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold

Cj1386 Is an Ankyrin-Containing Protein Involved in Heme Trafficking to Catalase in Campylobacter jejuni

Analysis of the LIV System of Campylobacter jejuni Reveals Alternative Roles for LivJ and LivK in Commensalism beyond Branched-Chain Amino Acid Transport

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