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Global proteomic profiling of Yersinia ruckeri strains
Yersinia ruckeri is the causative agent of enteric redmouth disease (ERM) of salmonids. There is little information regarding the proteomics of Y. ruckeri. Herein, we perform whole protein identification and quantification of biotype 1 and biotype 2 strains of Y. ruckeri grown under standard culture...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5607619/ https://www.ncbi.nlm.nih.gov/pubmed/28931430 http://dx.doi.org/10.1186/s13567-017-0460-3 |
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author | Kumar, Gokhlesh Hummel, Karin Welch, Timothy J. Razzazi-Fazeli, Ebrahim El-Matbouli, Mansour |
author_facet | Kumar, Gokhlesh Hummel, Karin Welch, Timothy J. Razzazi-Fazeli, Ebrahim El-Matbouli, Mansour |
author_sort | Kumar, Gokhlesh |
collection | PubMed |
description | Yersinia ruckeri is the causative agent of enteric redmouth disease (ERM) of salmonids. There is little information regarding the proteomics of Y. ruckeri. Herein, we perform whole protein identification and quantification of biotype 1 and biotype 2 strains of Y. ruckeri grown under standard culture conditions using a shotgun proteomic approach. Proteins were extracted, digested and peptides were separated by a nano liquid chromatography system and analyzed with a high-resolution hybrid triple quadrupole time of flight mass spectrometer coupled via a nano ESI interface. SWATH-MS technology and sophisticated statistical analyses were used to identify proteome differences among virulent and avirulent strains. GO annotation, subcellular localization, virulence proteins and antibiotic resistance ontology were predicted using bioinformatic tools. A total of 1395 proteins were identified in the whole cell of Y. ruckeri. These included proteases, chaperones, cell division proteins, outer membrane proteins, lipoproteins, receptors, ion binding proteins, transporters and catalytic proteins. In virulent strains, a total of 16 proteins were upregulated including anti-sigma regulatory factor, arginine deiminase, phosphate-binding protein PstS and superoxide dismutase Cu–Zu. Additionally, several virulence proteins were predicted such as Clp and Lon pro-teases, TolB, PPIases, PstS, PhoP and LuxR family transcriptional regulators. These putative virulence proteins might be used for development of novel targets for treatment of ERM in fish. Our study represents one of the first global proteomic reference profiles of Y. ruckeri and this data can be accessed via ProteomeXchange with identifier PXD005439. These proteomic profiles elucidate proteomic mechanisms, pathogenicity, host-interactions, antibiotic resistance ontology and localization of Y. ruckeri proteins. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13567-017-0460-3) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5607619 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-56076192017-09-24 Global proteomic profiling of Yersinia ruckeri strains Kumar, Gokhlesh Hummel, Karin Welch, Timothy J. Razzazi-Fazeli, Ebrahim El-Matbouli, Mansour Vet Res Research Article Yersinia ruckeri is the causative agent of enteric redmouth disease (ERM) of salmonids. There is little information regarding the proteomics of Y. ruckeri. Herein, we perform whole protein identification and quantification of biotype 1 and biotype 2 strains of Y. ruckeri grown under standard culture conditions using a shotgun proteomic approach. Proteins were extracted, digested and peptides were separated by a nano liquid chromatography system and analyzed with a high-resolution hybrid triple quadrupole time of flight mass spectrometer coupled via a nano ESI interface. SWATH-MS technology and sophisticated statistical analyses were used to identify proteome differences among virulent and avirulent strains. GO annotation, subcellular localization, virulence proteins and antibiotic resistance ontology were predicted using bioinformatic tools. A total of 1395 proteins were identified in the whole cell of Y. ruckeri. These included proteases, chaperones, cell division proteins, outer membrane proteins, lipoproteins, receptors, ion binding proteins, transporters and catalytic proteins. In virulent strains, a total of 16 proteins were upregulated including anti-sigma regulatory factor, arginine deiminase, phosphate-binding protein PstS and superoxide dismutase Cu–Zu. Additionally, several virulence proteins were predicted such as Clp and Lon pro-teases, TolB, PPIases, PstS, PhoP and LuxR family transcriptional regulators. These putative virulence proteins might be used for development of novel targets for treatment of ERM in fish. Our study represents one of the first global proteomic reference profiles of Y. ruckeri and this data can be accessed via ProteomeXchange with identifier PXD005439. These proteomic profiles elucidate proteomic mechanisms, pathogenicity, host-interactions, antibiotic resistance ontology and localization of Y. ruckeri proteins. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13567-017-0460-3) contains supplementary material, which is available to authorized users. BioMed Central 2017-09-20 2017 /pmc/articles/PMC5607619/ /pubmed/28931430 http://dx.doi.org/10.1186/s13567-017-0460-3 Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Kumar, Gokhlesh Hummel, Karin Welch, Timothy J. Razzazi-Fazeli, Ebrahim El-Matbouli, Mansour Global proteomic profiling of Yersinia ruckeri strains |
title | Global proteomic profiling of Yersinia ruckeri strains |
title_full | Global proteomic profiling of Yersinia ruckeri strains |
title_fullStr | Global proteomic profiling of Yersinia ruckeri strains |
title_full_unstemmed | Global proteomic profiling of Yersinia ruckeri strains |
title_short | Global proteomic profiling of Yersinia ruckeri strains |
title_sort | global proteomic profiling of yersinia ruckeri strains |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5607619/ https://www.ncbi.nlm.nih.gov/pubmed/28931430 http://dx.doi.org/10.1186/s13567-017-0460-3 |
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