| 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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MedLine Citation:
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PMID: 21949065 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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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Authors:
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Deborah A Ribardo; David R Hendrixson |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. Date: 2011-09-23 |
Journal Detail:
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Title: Journal of bacteriology Volume: 193 ISSN: 1098-5530 ISO Abbreviation: J. Bacteriol. Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-10-31 Completed Date: 2011-12-14 Revised Date: 2012-05-01 |
Medline Journal Info:
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Nlm Unique ID: 2985120R Medline TA: J Bacteriol Country: United States |
Other Details:
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Languages: eng Pagination: 6233-43 Citation Subset: IM |
Affiliation:
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Department of Microbiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Room NL 4.138A, Dallas, TX 75390-9048, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids, Branched-Chain
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metabolism Animals Bacterial Proteins / genetics, metabolism* Biological Transport Campylobacter Infections / microbiology Campylobacter jejuni / genetics, physiology* Chickens / microbiology, physiology* Humans Intestines / microbiology, physiology Isoleucine / metabolism Leucine / metabolism Periplasmic Binding Proteins / genetics, metabolism* Symbiosis* Valine / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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R01 AI065539/AI/NIAID NIH HHS; R01 AI065539-06/AI/NIAID NIH HHS; R01 AI065539-07/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids, Branched-Chain; 0/Bacterial Proteins; 0/Periplasmic Binding Proteins; 61-90-5/Leucine; 7004-03-7/Valine; 73-32-5/Isoleucine |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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