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Proteomic Investigation of the Response of Enterococcus faecalis V583 when Cultivated in Urine

Enterococcus faecalis is a robust bacterium, which is able to survive in and adapt to hostile environments such as the urinary tract and bladder. In this label-free quantitative proteomic study based on MaxQuant LFQ algorithms, we identified 127 proteins present in the secretome of the clinical vanc...

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Autores principales: Arntzen, Magnus Øverlie, Karlskås, Ingrid Lea, Skaugen, Morten, Eijsink, Vincent G. H., Mathiesen, Geir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4411035/
https://www.ncbi.nlm.nih.gov/pubmed/25915650
http://dx.doi.org/10.1371/journal.pone.0126694
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author Arntzen, Magnus Øverlie
Karlskås, Ingrid Lea
Skaugen, Morten
Eijsink, Vincent G. H.
Mathiesen, Geir
author_facet Arntzen, Magnus Øverlie
Karlskås, Ingrid Lea
Skaugen, Morten
Eijsink, Vincent G. H.
Mathiesen, Geir
author_sort Arntzen, Magnus Øverlie
collection PubMed
description Enterococcus faecalis is a robust bacterium, which is able to survive in and adapt to hostile environments such as the urinary tract and bladder. In this label-free quantitative proteomic study based on MaxQuant LFQ algorithms, we identified 127 proteins present in the secretome of the clinical vancomycin-resistant isolate E. faecalis V583 and we compared proteins secreted in the initial phase of cultivation in urine with the secretome during cultivation in standard laboratory medium, 2xYT. Of the 54 identified proteins predicted to be secreted, six were exclusively found after cultivation in urine including the virulence factor EfaA (“endocarditis specific antigen”) and its homologue EF0577 (“adhesion lipoprotein”). These two proteins are both involved in manganese transport, known to be an important determinant of colonization and infection, and may additionally function as adhesins. Other detected urine-specific proteins are involved in peptide transport (EF0063 and EF3106) and protease inhibition (EF3054). In addition, we found an uncharacterized protein (EF0764), which had not previously been linked to the adaptation of V583 to a urine environment, and which is unique to E. faecalis. Proteins found in both environments included a histone-like protein, EF1550, that was up-regulated during cultivation in urine and that has a homologue in streptococci (HlpA) known to be involved in bacterial adhesion to host cells. Up-regulated secreted proteins included autolysins. These results from secretome analyses are largely compatible with previously published data from transcriptomics studies. All in all, the present data indicate that transport, in particular metal transport, adhesion, cell wall remodelling and the unknown function carried out by the unique EF0764 are important for enterococcal adaptation to the urine environment. These results provide a basis for a more targeted exploration of novel proteins involved in the adaptability and pathogenicity of E. faecalis.
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spelling pubmed-44110352015-05-07 Proteomic Investigation of the Response of Enterococcus faecalis V583 when Cultivated in Urine Arntzen, Magnus Øverlie Karlskås, Ingrid Lea Skaugen, Morten Eijsink, Vincent G. H. Mathiesen, Geir PLoS One Research Article Enterococcus faecalis is a robust bacterium, which is able to survive in and adapt to hostile environments such as the urinary tract and bladder. In this label-free quantitative proteomic study based on MaxQuant LFQ algorithms, we identified 127 proteins present in the secretome of the clinical vancomycin-resistant isolate E. faecalis V583 and we compared proteins secreted in the initial phase of cultivation in urine with the secretome during cultivation in standard laboratory medium, 2xYT. Of the 54 identified proteins predicted to be secreted, six were exclusively found after cultivation in urine including the virulence factor EfaA (“endocarditis specific antigen”) and its homologue EF0577 (“adhesion lipoprotein”). These two proteins are both involved in manganese transport, known to be an important determinant of colonization and infection, and may additionally function as adhesins. Other detected urine-specific proteins are involved in peptide transport (EF0063 and EF3106) and protease inhibition (EF3054). In addition, we found an uncharacterized protein (EF0764), which had not previously been linked to the adaptation of V583 to a urine environment, and which is unique to E. faecalis. Proteins found in both environments included a histone-like protein, EF1550, that was up-regulated during cultivation in urine and that has a homologue in streptococci (HlpA) known to be involved in bacterial adhesion to host cells. Up-regulated secreted proteins included autolysins. These results from secretome analyses are largely compatible with previously published data from transcriptomics studies. All in all, the present data indicate that transport, in particular metal transport, adhesion, cell wall remodelling and the unknown function carried out by the unique EF0764 are important for enterococcal adaptation to the urine environment. These results provide a basis for a more targeted exploration of novel proteins involved in the adaptability and pathogenicity of E. faecalis. Public Library of Science 2015-04-27 /pmc/articles/PMC4411035/ /pubmed/25915650 http://dx.doi.org/10.1371/journal.pone.0126694 Text en © 2015 Arntzen 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, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Arntzen, Magnus Øverlie
Karlskås, Ingrid Lea
Skaugen, Morten
Eijsink, Vincent G. H.
Mathiesen, Geir
Proteomic Investigation of the Response of Enterococcus faecalis V583 when Cultivated in Urine
title Proteomic Investigation of the Response of Enterococcus faecalis V583 when Cultivated in Urine
title_full Proteomic Investigation of the Response of Enterococcus faecalis V583 when Cultivated in Urine
title_fullStr Proteomic Investigation of the Response of Enterococcus faecalis V583 when Cultivated in Urine
title_full_unstemmed Proteomic Investigation of the Response of Enterococcus faecalis V583 when Cultivated in Urine
title_short Proteomic Investigation of the Response of Enterococcus faecalis V583 when Cultivated in Urine
title_sort proteomic investigation of the response of enterococcus faecalis v583 when cultivated in urine
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4411035/
https://www.ncbi.nlm.nih.gov/pubmed/25915650
http://dx.doi.org/10.1371/journal.pone.0126694
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