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Characterization of the Opp Peptide Transporter of Corynebacterium pseudotuberculosis and Its Role in Virulence and Pathogenicity

Despite the economic importance of caseous lymphadenitis (CLA), a chronic disease caused by Corynebacterium pseudotuberculosis, few genes related to the virulence of its etiologic agent have been characterized. The oligopeptide permease (Opp) transporters are located in the plasma membrane and have...

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Autores principales: Moraes, Pablo M. R. O., Seyffert, Nubia, Silva, Wanderson M., Castro, Thiago L. P., Silva, Renata F., Lima, Danielle D., Hirata, Raphael, Silva, Artur, Miyoshi, Anderson, Azevedo, Vasco
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4034477/
https://www.ncbi.nlm.nih.gov/pubmed/24895581
http://dx.doi.org/10.1155/2014/489782
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author Moraes, Pablo M. R. O.
Seyffert, Nubia
Silva, Wanderson M.
Castro, Thiago L. P.
Silva, Renata F.
Lima, Danielle D.
Hirata, Raphael
Silva, Artur
Miyoshi, Anderson
Azevedo, Vasco
author_facet Moraes, Pablo M. R. O.
Seyffert, Nubia
Silva, Wanderson M.
Castro, Thiago L. P.
Silva, Renata F.
Lima, Danielle D.
Hirata, Raphael
Silva, Artur
Miyoshi, Anderson
Azevedo, Vasco
author_sort Moraes, Pablo M. R. O.
collection PubMed
description Despite the economic importance of caseous lymphadenitis (CLA), a chronic disease caused by Corynebacterium pseudotuberculosis, few genes related to the virulence of its etiologic agent have been characterized. The oligopeptide permease (Opp) transporters are located in the plasma membrane and have functions generally related to the uptake of peptides from the extracellular environment. These peptide transporters, in addition to having an important role in cell nutrition, also participate in the regulation of various processes involving intercellular signaling, including the control of the expression of virulence genes in pathogenic bacteria. To study the role of Opp in C. pseudotuberculosis, an OppD deficient strain was constructed via simple crossover with a nonreplicative plasmid carrying part of the oppD gene sequence. As occurred to the wild-type, the ΔoppD strain showed impaired growth when exposed to the toxic glutathione peptide (GSH), indicating two possible scenarios: (i) that this component can be internalized by the bacterium through an Opp-independent pathway or (ii) that there is toxicity while the peptide is extracellular. Additionally, the ΔoppD mutant presented a reduced ability to adhere to and infect macrophages compared to the wild-type, although both strains exhibit the same potential to colonize spleens and cause injury and death to infected mice.
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spelling pubmed-40344772014-06-03 Characterization of the Opp Peptide Transporter of Corynebacterium pseudotuberculosis and Its Role in Virulence and Pathogenicity Moraes, Pablo M. R. O. Seyffert, Nubia Silva, Wanderson M. Castro, Thiago L. P. Silva, Renata F. Lima, Danielle D. Hirata, Raphael Silva, Artur Miyoshi, Anderson Azevedo, Vasco Biomed Res Int Research Article Despite the economic importance of caseous lymphadenitis (CLA), a chronic disease caused by Corynebacterium pseudotuberculosis, few genes related to the virulence of its etiologic agent have been characterized. The oligopeptide permease (Opp) transporters are located in the plasma membrane and have functions generally related to the uptake of peptides from the extracellular environment. These peptide transporters, in addition to having an important role in cell nutrition, also participate in the regulation of various processes involving intercellular signaling, including the control of the expression of virulence genes in pathogenic bacteria. To study the role of Opp in C. pseudotuberculosis, an OppD deficient strain was constructed via simple crossover with a nonreplicative plasmid carrying part of the oppD gene sequence. As occurred to the wild-type, the ΔoppD strain showed impaired growth when exposed to the toxic glutathione peptide (GSH), indicating two possible scenarios: (i) that this component can be internalized by the bacterium through an Opp-independent pathway or (ii) that there is toxicity while the peptide is extracellular. Additionally, the ΔoppD mutant presented a reduced ability to adhere to and infect macrophages compared to the wild-type, although both strains exhibit the same potential to colonize spleens and cause injury and death to infected mice. Hindawi Publishing Corporation 2014 2014-05-08 /pmc/articles/PMC4034477/ /pubmed/24895581 http://dx.doi.org/10.1155/2014/489782 Text en Copyright © 2014 Pablo M. R. O. Moraes et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Moraes, Pablo M. R. O.
Seyffert, Nubia
Silva, Wanderson M.
Castro, Thiago L. P.
Silva, Renata F.
Lima, Danielle D.
Hirata, Raphael
Silva, Artur
Miyoshi, Anderson
Azevedo, Vasco
Characterization of the Opp Peptide Transporter of Corynebacterium pseudotuberculosis and Its Role in Virulence and Pathogenicity
title Characterization of the Opp Peptide Transporter of Corynebacterium pseudotuberculosis and Its Role in Virulence and Pathogenicity
title_full Characterization of the Opp Peptide Transporter of Corynebacterium pseudotuberculosis and Its Role in Virulence and Pathogenicity
title_fullStr Characterization of the Opp Peptide Transporter of Corynebacterium pseudotuberculosis and Its Role in Virulence and Pathogenicity
title_full_unstemmed Characterization of the Opp Peptide Transporter of Corynebacterium pseudotuberculosis and Its Role in Virulence and Pathogenicity
title_short Characterization of the Opp Peptide Transporter of Corynebacterium pseudotuberculosis and Its Role in Virulence and Pathogenicity
title_sort characterization of the opp peptide transporter of corynebacterium pseudotuberculosis and its role in virulence and pathogenicity
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4034477/
https://www.ncbi.nlm.nih.gov/pubmed/24895581
http://dx.doi.org/10.1155/2014/489782
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