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Salmonella Typhi, Paratyphi A, Enteritidis and Typhimurium core proteomes reveal differentially expressed proteins linked to the cell surface and pathogenicity

BACKGROUND: Salmonella enterica subsp. enterica contains more than 2,600 serovars of which four are of major medical relevance for humans. While the typhoidal serovars (Typhi and Paratyphi A) are human-restricted and cause enteric fever, non-typhoidal Salmonella serovars (Typhimurium and Enteritidis...

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Autores principales: Saleh, Sara, Van Puyvelde, Sandra, Staes, An, Timmerman, Evy, Barbé, Barbara, Jacobs, Jan, Gevaert, Kris, Deborggraeve, Stijn
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6553789/
https://www.ncbi.nlm.nih.gov/pubmed/31125353
http://dx.doi.org/10.1371/journal.pntd.0007416
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author Saleh, Sara
Van Puyvelde, Sandra
Staes, An
Timmerman, Evy
Barbé, Barbara
Jacobs, Jan
Gevaert, Kris
Deborggraeve, Stijn
author_facet Saleh, Sara
Van Puyvelde, Sandra
Staes, An
Timmerman, Evy
Barbé, Barbara
Jacobs, Jan
Gevaert, Kris
Deborggraeve, Stijn
author_sort Saleh, Sara
collection PubMed
description BACKGROUND: Salmonella enterica subsp. enterica contains more than 2,600 serovars of which four are of major medical relevance for humans. While the typhoidal serovars (Typhi and Paratyphi A) are human-restricted and cause enteric fever, non-typhoidal Salmonella serovars (Typhimurium and Enteritidis) have a broad host range and predominantly cause gastroenteritis. METHODOLOGY/PRINCIPLE FINDINGS: We compared the core proteomes of Salmonella Typhi, Paratyphi A, Typhimurium and Enteritidis using contemporary proteomics. For each serovar, five clinical isolates (covering different geographical origins) and one reference strain were grown in vitro to the exponential phase. Levels of orthologous proteins quantified in all four serovars and within the typhoidal and non-typhoidal groups were compared and subjected to gene ontology term enrichment and inferred regulatory interactions. Differential expression of the core proteomes of the typhoidal serovars appears mainly related to cell surface components and, for the non-typhoidal serovars, to pathogenicity. CONCLUSIONS/SIGNIFICANCE: Our comparative proteome analysis indicated differences in the expression of surface proteins between Salmonella Typhi and Paratyphi A, and in pathogenesis-related proteins between Salmonella Typhimurium and Enteritidis. Our findings may guide future development of novel diagnostics and vaccines, as well as understanding of disease progression.
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spelling pubmed-65537892019-06-17 Salmonella Typhi, Paratyphi A, Enteritidis and Typhimurium core proteomes reveal differentially expressed proteins linked to the cell surface and pathogenicity Saleh, Sara Van Puyvelde, Sandra Staes, An Timmerman, Evy Barbé, Barbara Jacobs, Jan Gevaert, Kris Deborggraeve, Stijn PLoS Negl Trop Dis Research Article BACKGROUND: Salmonella enterica subsp. enterica contains more than 2,600 serovars of which four are of major medical relevance for humans. While the typhoidal serovars (Typhi and Paratyphi A) are human-restricted and cause enteric fever, non-typhoidal Salmonella serovars (Typhimurium and Enteritidis) have a broad host range and predominantly cause gastroenteritis. METHODOLOGY/PRINCIPLE FINDINGS: We compared the core proteomes of Salmonella Typhi, Paratyphi A, Typhimurium and Enteritidis using contemporary proteomics. For each serovar, five clinical isolates (covering different geographical origins) and one reference strain were grown in vitro to the exponential phase. Levels of orthologous proteins quantified in all four serovars and within the typhoidal and non-typhoidal groups were compared and subjected to gene ontology term enrichment and inferred regulatory interactions. Differential expression of the core proteomes of the typhoidal serovars appears mainly related to cell surface components and, for the non-typhoidal serovars, to pathogenicity. CONCLUSIONS/SIGNIFICANCE: Our comparative proteome analysis indicated differences in the expression of surface proteins between Salmonella Typhi and Paratyphi A, and in pathogenesis-related proteins between Salmonella Typhimurium and Enteritidis. Our findings may guide future development of novel diagnostics and vaccines, as well as understanding of disease progression. Public Library of Science 2019-05-24 /pmc/articles/PMC6553789/ /pubmed/31125353 http://dx.doi.org/10.1371/journal.pntd.0007416 Text en © 2019 Saleh et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Saleh, Sara
Van Puyvelde, Sandra
Staes, An
Timmerman, Evy
Barbé, Barbara
Jacobs, Jan
Gevaert, Kris
Deborggraeve, Stijn
Salmonella Typhi, Paratyphi A, Enteritidis and Typhimurium core proteomes reveal differentially expressed proteins linked to the cell surface and pathogenicity
title Salmonella Typhi, Paratyphi A, Enteritidis and Typhimurium core proteomes reveal differentially expressed proteins linked to the cell surface and pathogenicity
title_full Salmonella Typhi, Paratyphi A, Enteritidis and Typhimurium core proteomes reveal differentially expressed proteins linked to the cell surface and pathogenicity
title_fullStr Salmonella Typhi, Paratyphi A, Enteritidis and Typhimurium core proteomes reveal differentially expressed proteins linked to the cell surface and pathogenicity
title_full_unstemmed Salmonella Typhi, Paratyphi A, Enteritidis and Typhimurium core proteomes reveal differentially expressed proteins linked to the cell surface and pathogenicity
title_short Salmonella Typhi, Paratyphi A, Enteritidis and Typhimurium core proteomes reveal differentially expressed proteins linked to the cell surface and pathogenicity
title_sort salmonella typhi, paratyphi a, enteritidis and typhimurium core proteomes reveal differentially expressed proteins linked to the cell surface and pathogenicity
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6553789/
https://www.ncbi.nlm.nih.gov/pubmed/31125353
http://dx.doi.org/10.1371/journal.pntd.0007416
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