The Enterococcus faecalis Exoproteome: Identification and Temporal Regulation by Fsr

Analysis of the culture supernatant exoproteins produced by two PFGE clusters of high-level gentamicin and ciprofloxacin-resistant clinical isolates of Enterococcus faecalis from the UK and Ireland revealed two distinct protein profiles. This grouping distinguished OG1RF and GelE metalloprotease-exp...

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Main Authors:	Shankar, Jayendra, Walker, Rachel G., Ward, Deborah, Horsburgh, Malcolm J.
Format:	Online
Language:	English
Published:	Public Library of Science 2012
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3299793/

id	pubmed-3299793
recordtype	oai_dc
spelling	pubmed-32997932012-03-16 The Enterococcus faecalis Exoproteome: Identification and Temporal Regulation by Fsr Shankar, Jayendra Walker, Rachel G. Ward, Deborah Horsburgh, Malcolm J. Research Article Analysis of the culture supernatant exoproteins produced by two PFGE clusters of high-level gentamicin and ciprofloxacin-resistant clinical isolates of Enterococcus faecalis from the UK and Ireland revealed two distinct protein profiles. This grouping distinguished OG1RF and GelE metalloprotease-expressing isolates from JH2-2 and other GelE-negative isolates. The integrity of the fsrABDC operon was found to determine the exoproteome composition, since an fsrB mutant of strain OG1RF appeared very similar to that of strain JH2-2, and complementation of the latter with the fsrABDC operon produced an OG1RF-like exoproteome. The proteins present in the supernatant fraction of OG1RF were separated using 2D gels and identified by mass spectrometry and comprised many mass and pI variants of the GelE and SprE proteases. In addition cell wall synthesis and cell division proteins were identified. An OG1RF fsrB mutant had a distinct exoprotein fraction with an absence of the Fsr-regulated proteases and was characterised by general stress and glycolytic proteins. The exoproteome of the OG1RF fsrB mutant resembles that of a divIVA mutant of E. faecalis, suggestive of a stress phenotype. Public Library of Science 2012-03-12 /pmc/articles/PMC3299793/ /pubmed/22428053 http://dx.doi.org/10.1371/journal.pone.0033450 Text en Shankar 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.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Shankar, Jayendra Walker, Rachel G. Ward, Deborah Horsburgh, Malcolm J.
spellingShingle	Shankar, Jayendra Walker, Rachel G. Ward, Deborah Horsburgh, Malcolm J. The Enterococcus faecalis Exoproteome: Identification and Temporal Regulation by Fsr
author_facet	Shankar, Jayendra Walker, Rachel G. Ward, Deborah Horsburgh, Malcolm J.
author_sort	Shankar, Jayendra
title	The Enterococcus faecalis Exoproteome: Identification and Temporal Regulation by Fsr
title_short	The Enterococcus faecalis Exoproteome: Identification and Temporal Regulation by Fsr
title_full	The Enterococcus faecalis Exoproteome: Identification and Temporal Regulation by Fsr
title_fullStr	The Enterococcus faecalis Exoproteome: Identification and Temporal Regulation by Fsr
title_full_unstemmed	The Enterococcus faecalis Exoproteome: Identification and Temporal Regulation by Fsr
title_sort	enterococcus faecalis exoproteome: identification and temporal regulation by fsr
description	Analysis of the culture supernatant exoproteins produced by two PFGE clusters of high-level gentamicin and ciprofloxacin-resistant clinical isolates of Enterococcus faecalis from the UK and Ireland revealed two distinct protein profiles. This grouping distinguished OG1RF and GelE metalloprotease-expressing isolates from JH2-2 and other GelE-negative isolates. The integrity of the fsrABDC operon was found to determine the exoproteome composition, since an fsrB mutant of strain OG1RF appeared very similar to that of strain JH2-2, and complementation of the latter with the fsrABDC operon produced an OG1RF-like exoproteome. The proteins present in the supernatant fraction of OG1RF were separated using 2D gels and identified by mass spectrometry and comprised many mass and pI variants of the GelE and SprE proteases. In addition cell wall synthesis and cell division proteins were identified. An OG1RF fsrB mutant had a distinct exoprotein fraction with an absence of the Fsr-regulated proteases and was characterised by general stress and glycolytic proteins. The exoproteome of the OG1RF fsrB mutant resembles that of a divIVA mutant of E. faecalis, suggestive of a stress phenotype.
publisher	Public Library of Science
publishDate	2012
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3299793/
_version_	1611512362760667136

The Enterococcus faecalis Exoproteome: Identification and Temporal Regulation by Fsr

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