Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization.

Hdl Handle:
http://hdl.handle.net/10675.2/106
Title:
Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization.
Authors:
Rathbun, Kimberly M; Hall, Johanna E; Thompson, Stuart A
Abstract:
BACKGROUND: Campylobacter jejuni is a gastrointestinal pathogen of humans, but part of the normal flora of poultry, and therefore grows well at the respective body temperatures of 37 degrees C and 42 degrees C. Proteomic studies on temperature regulation in C. jejuni strain 81-176 revealed the upregulation at 37 degrees C of Cj0596, a predicted periplasmic chaperone that is similar to proteins involved in outer membrane protein folding and virulence in other bacteria. RESULTS: The cj0596 gene was highly conserved in 24 strains and species of Campylobacter, implying the importance of this gene. To study the role that Cj0596 plays in C. jejuni pathogenesis, a mutant derivative of strain 81-176 was constructed in which the cj0596 gene was precisely deleted. A revertant of this mutant was isolated by restoring the gene to its original chromosomal location using streptomycin counterselection. The cj0596 mutant strain demonstrated a slightly decreased growth rate and lower final growth yield, yet was more motile and more invasive of human intestinal epithelial cells than wild-type. In either single or mixed infections, the mutant was less able to colonize mice than 81-176. The cj0596 mutant also expressed altered levels of several proteins. CONCLUSION: Mutation of cj0596 has an effect on phenotypes related to C. jejuni pathogenesis, probably due to its role in the proper folding of critical outer membrane proteins.
Citation:
BMC Microbiol. 2009 Aug 8; 9:160
Issue Date:
31-Aug-2009
URI:
http://hdl.handle.net/10675.2/106
DOI:
10.1186/1471-2180-9-160
PubMed ID:
19664234
PubMed Central ID:
PMC2782263
Type:
Journal Article; Research Support, N.I.H., Extramural
ISSN:
1471-2180
Appears in Collections:
Department of Biochemistry and Molecular Biology: Faculty Research and Presentations

Full metadata record

DC FieldValue Language
dc.contributor.authorRathbun, Kimberly Men_US
dc.contributor.authorHall, Johanna Een_US
dc.contributor.authorThompson, Stuart Aen_US
dc.date.accessioned2010-09-24T22:03:20Z-
dc.date.available2010-09-24T22:03:20Z-
dc.date.issued2009-08-31en_US
dc.identifier.citationBMC Microbiol. 2009 Aug 8; 9:160en_US
dc.identifier.issn1471-2180en_US
dc.identifier.pmid19664234en_US
dc.identifier.doi10.1186/1471-2180-9-160en_US
dc.identifier.urihttp://hdl.handle.net/10675.2/106-
dc.description.abstractBACKGROUND: Campylobacter jejuni is a gastrointestinal pathogen of humans, but part of the normal flora of poultry, and therefore grows well at the respective body temperatures of 37 degrees C and 42 degrees C. Proteomic studies on temperature regulation in C. jejuni strain 81-176 revealed the upregulation at 37 degrees C of Cj0596, a predicted periplasmic chaperone that is similar to proteins involved in outer membrane protein folding and virulence in other bacteria. RESULTS: The cj0596 gene was highly conserved in 24 strains and species of Campylobacter, implying the importance of this gene. To study the role that Cj0596 plays in C. jejuni pathogenesis, a mutant derivative of strain 81-176 was constructed in which the cj0596 gene was precisely deleted. A revertant of this mutant was isolated by restoring the gene to its original chromosomal location using streptomycin counterselection. The cj0596 mutant strain demonstrated a slightly decreased growth rate and lower final growth yield, yet was more motile and more invasive of human intestinal epithelial cells than wild-type. In either single or mixed infections, the mutant was less able to colonize mice than 81-176. The cj0596 mutant also expressed altered levels of several proteins. CONCLUSION: Mutation of cj0596 has an effect on phenotypes related to C. jejuni pathogenesis, probably due to its role in the proper folding of critical outer membrane proteins.en_US
dc.rightsThe PMC Open Access Subset is a relatively small part of the total collection of articles in PMC. Articles in the PMC Open Access Subset are still protected by copyright, but are made available under a Creative Commons or similar license that generally allows more liberal redistribution and reuse than a traditional copyrighted work. Please refer to the license statement in each article for specific terms of use. The license terms are not identical for all articles in this subset.en_US
dc.subject.meshAnimalsen_US
dc.subject.meshBacterial Proteins / genetics / metabolismen_US
dc.subject.meshCampylobacter Infections / microbiologyen_US
dc.subject.meshCampylobacter jejuni / enzymology / genetics / pathogenicityen_US
dc.subject.meshCell Lineen_US
dc.subject.meshFemaleen_US
dc.subject.meshGene Deletionen_US
dc.subject.meshHumansen_US
dc.subject.meshMiceen_US
dc.subject.meshMice, Inbred BALB Cen_US
dc.subject.meshPeptidylprolyl Isomerase / genetics / metabolismen_US
dc.subject.meshPeriplasmic Proteins / genetics / metabolismen_US
dc.subject.meshPhenotypeen_US
dc.subject.meshProteome / metabolismen_US
dc.titleCj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, N.I.H., Extramuralen_US
dc.identifier.pmcidPMC2782263en_US
dc.contributor.corporatenameDepartment of Biochemistry and Molecular Biologyen_US

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