Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.

<h4>Background</h4>Bacterial Dsb enzymes are involved in the oxidative folding of many proteins, through the formation of disulfide bonds between their cysteine residues. The Dsb protein network has been well characterized in cells of the model microorganism Escherichia coli. To gain ins...

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Autores principales:	Anna D Grabowska, Ewa Wywiał, Stanislaw Dunin-Horkawicz, Anna M Łasica, Marc M S M Wösten, Anna Nagy-Staroń, Renata Godlewska, Katarzyna Bocian-Ostrzycka, Katarzyna Pieńkowska, Paweł Łaniewski, Janusz M Bujnicki, Jos P M van Putten, E Katarzyna Jagusztyn-Krynicka
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/609ae1e86bf142ebae9cc4a71fdcee8b
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spelling	oai:doaj.org-article:609ae1e86bf142ebae9cc4a71fdcee8b2021-11-25T06:02:15ZFunctional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.1932-620310.1371/journal.pone.0106247https://doaj.org/article/609ae1e86bf142ebae9cc4a71fdcee8b2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25181355/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Bacterial Dsb enzymes are involved in the oxidative folding of many proteins, through the formation of disulfide bonds between their cysteine residues. The Dsb protein network has been well characterized in cells of the model microorganism Escherichia coli. To gain insight into the functioning of the Dsb system in epsilon-Proteobacteria, where it plays an important role in the colonization process, we studied two homologs of the main Escherichia coli Dsb oxidase (EcDsbA) that are present in the cells of the enteric pathogen Campylobacter jejuni, the most frequently reported bacterial cause of human enteritis in the world.<h4>Methods and results</h4>Phylogenetic analysis suggests the horizontal transfer of the epsilon-Proteobacterial DsbAs from a common ancestor to gamma-Proteobacteria, which then gave rise to the DsbL lineage. Phenotype and enzymatic assays suggest that the two C. jejuni DsbAs play different roles in bacterial cells and have divergent substrate spectra. CjDsbA1 is essential for the motility and autoagglutination phenotypes, while CjDsbA2 has no impact on those processes. CjDsbA1 plays a critical role in the oxidative folding that ensures the activity of alkaline phosphatase CjPhoX, whereas CjDsbA2 is crucial for the activity of arylsulfotransferase CjAstA, encoded within the dsbA2-dsbB-astA operon.<h4>Conclusions</h4>Our results show that CjDsbA1 is the primary thiol-oxidoreductase affecting life processes associated with bacterial spread and host colonization, as well as ensuring the oxidative folding of particular protein substrates. In contrast, CjDsbA2 activity does not affect the same processes and so far its oxidative folding activity has been demonstrated for one substrate, arylsulfotransferase CjAstA. The results suggest the cooperation between CjDsbA2 and CjDsbB. In the case of the CjDsbA1, this cooperation is not exclusive and there is probably another protein to be identified in C. jejuni cells that acts to re-oxidize CjDsbA1. Altogether the data presented here constitute the considerable insight to the Epsilonproteobacterial Dsb systems, which have been poorly understood so far.Anna D GrabowskaEwa WywiałStanislaw Dunin-HorkawiczAnna M ŁasicaMarc M S M WöstenAnna Nagy-StarońRenata GodlewskaKatarzyna Bocian-OstrzyckaKatarzyna PieńkowskaPaweł ŁaniewskiJanusz M BujnickiJos P M van PuttenE Katarzyna Jagusztyn-KrynickaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 9, p e106247 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anna D Grabowska Ewa Wywiał Stanislaw Dunin-Horkawicz Anna M Łasica Marc M S M Wösten Anna Nagy-Staroń Renata Godlewska Katarzyna Bocian-Ostrzycka Katarzyna Pieńkowska Paweł Łaniewski Janusz M Bujnicki Jos P M van Putten E Katarzyna Jagusztyn-Krynicka Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.
description	<h4>Background</h4>Bacterial Dsb enzymes are involved in the oxidative folding of many proteins, through the formation of disulfide bonds between their cysteine residues. The Dsb protein network has been well characterized in cells of the model microorganism Escherichia coli. To gain insight into the functioning of the Dsb system in epsilon-Proteobacteria, where it plays an important role in the colonization process, we studied two homologs of the main Escherichia coli Dsb oxidase (EcDsbA) that are present in the cells of the enteric pathogen Campylobacter jejuni, the most frequently reported bacterial cause of human enteritis in the world.<h4>Methods and results</h4>Phylogenetic analysis suggests the horizontal transfer of the epsilon-Proteobacterial DsbAs from a common ancestor to gamma-Proteobacteria, which then gave rise to the DsbL lineage. Phenotype and enzymatic assays suggest that the two C. jejuni DsbAs play different roles in bacterial cells and have divergent substrate spectra. CjDsbA1 is essential for the motility and autoagglutination phenotypes, while CjDsbA2 has no impact on those processes. CjDsbA1 plays a critical role in the oxidative folding that ensures the activity of alkaline phosphatase CjPhoX, whereas CjDsbA2 is crucial for the activity of arylsulfotransferase CjAstA, encoded within the dsbA2-dsbB-astA operon.<h4>Conclusions</h4>Our results show that CjDsbA1 is the primary thiol-oxidoreductase affecting life processes associated with bacterial spread and host colonization, as well as ensuring the oxidative folding of particular protein substrates. In contrast, CjDsbA2 activity does not affect the same processes and so far its oxidative folding activity has been demonstrated for one substrate, arylsulfotransferase CjAstA. The results suggest the cooperation between CjDsbA2 and CjDsbB. In the case of the CjDsbA1, this cooperation is not exclusive and there is probably another protein to be identified in C. jejuni cells that acts to re-oxidize CjDsbA1. Altogether the data presented here constitute the considerable insight to the Epsilonproteobacterial Dsb systems, which have been poorly understood so far.
format	article
author	Anna D Grabowska Ewa Wywiał Stanislaw Dunin-Horkawicz Anna M Łasica Marc M S M Wösten Anna Nagy-Staroń Renata Godlewska Katarzyna Bocian-Ostrzycka Katarzyna Pieńkowska Paweł Łaniewski Janusz M Bujnicki Jos P M van Putten E Katarzyna Jagusztyn-Krynicka
author_facet	Anna D Grabowska Ewa Wywiał Stanislaw Dunin-Horkawicz Anna M Łasica Marc M S M Wösten Anna Nagy-Staroń Renata Godlewska Katarzyna Bocian-Ostrzycka Katarzyna Pieńkowska Paweł Łaniewski Janusz M Bujnicki Jos P M van Putten E Katarzyna Jagusztyn-Krynicka
author_sort	Anna D Grabowska
title	Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.
title_short	Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.
title_full	Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.
title_fullStr	Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.
title_full_unstemmed	Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.
title_sort	functional and bioinformatics analysis of two campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, dsba.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/609ae1e86bf142ebae9cc4a71fdcee8b
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Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.

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