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Enterococcus faecalis V583 cell membrane protein expression to alkaline stress

Enterococcus faecalis is able to adapt to alkaline conditions and is commonly recovered from teeth in which endodontic treatment has failed. The role that E. faecalis membrane proteins play in survival strategies to extreme alkaline conditions is unclear. We grew E. faecalis V583 in a chemostat at p...

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Autores principales: Cathro, Peter, McCarthy, Peter, Hoffmann, Peter, Kidd, Stephen, Zilm, Peter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9491840/
https://www.ncbi.nlm.nih.gov/pubmed/36044998
http://dx.doi.org/10.1093/femsle/fnac082
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author Cathro, Peter
McCarthy, Peter
Hoffmann, Peter
Kidd, Stephen
Zilm, Peter
author_facet Cathro, Peter
McCarthy, Peter
Hoffmann, Peter
Kidd, Stephen
Zilm, Peter
author_sort Cathro, Peter
collection PubMed
description Enterococcus faecalis is able to adapt to alkaline conditions and is commonly recovered from teeth in which endodontic treatment has failed. The role that E. faecalis membrane proteins play in survival strategies to extreme alkaline conditions is unclear. We grew E. faecalis V583 in a chemostat at pH 8 and 11 at one-tenth the organism’s relative maximum growth rate. Following membrane shaving, isotope-coding protein labels were added at the peptide level to samples and then combined. The relative proportion of membrane proteins were identified using LC-ESI mass spectrometry and MaxQuant analysis. Ratios of membrane proteins were log(2) transformed, with proteins deviating by more than 1 SD of the mean considered to be up- or down-regulated. A total of six proteins were up-regulated in pH 11 including: EF0669 (polysaccharide biosynthesis family); EF1927 (glycerol uptake facilitator), and EF0114 (glycosyl hydrolase). A total of five proteins were down-regulated including: EF0108 (C4-dicarboxylate transporter); EF1838 (PTS system IIC component); EF0456 (PTS system IID component); and EF0022 (PTS mannose-specific IID component). In extreme alkaline conditions, the membrane proteins of E. faecalis seem to be involved in a shift of carbohydrate metabolism from the PTS system to glycerol, which supports the formation of a protective capsule protecting the cell.
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spelling pubmed-94918402022-09-22 Enterococcus faecalis V583 cell membrane protein expression to alkaline stress Cathro, Peter McCarthy, Peter Hoffmann, Peter Kidd, Stephen Zilm, Peter FEMS Microbiol Lett Research Letter Enterococcus faecalis is able to adapt to alkaline conditions and is commonly recovered from teeth in which endodontic treatment has failed. The role that E. faecalis membrane proteins play in survival strategies to extreme alkaline conditions is unclear. We grew E. faecalis V583 in a chemostat at pH 8 and 11 at one-tenth the organism’s relative maximum growth rate. Following membrane shaving, isotope-coding protein labels were added at the peptide level to samples and then combined. The relative proportion of membrane proteins were identified using LC-ESI mass spectrometry and MaxQuant analysis. Ratios of membrane proteins were log(2) transformed, with proteins deviating by more than 1 SD of the mean considered to be up- or down-regulated. A total of six proteins were up-regulated in pH 11 including: EF0669 (polysaccharide biosynthesis family); EF1927 (glycerol uptake facilitator), and EF0114 (glycosyl hydrolase). A total of five proteins were down-regulated including: EF0108 (C4-dicarboxylate transporter); EF1838 (PTS system IIC component); EF0456 (PTS system IID component); and EF0022 (PTS mannose-specific IID component). In extreme alkaline conditions, the membrane proteins of E. faecalis seem to be involved in a shift of carbohydrate metabolism from the PTS system to glycerol, which supports the formation of a protective capsule protecting the cell. Oxford University Press 2022-08-31 /pmc/articles/PMC9491840/ /pubmed/36044998 http://dx.doi.org/10.1093/femsle/fnac082 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of FEMS. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Research Letter
Cathro, Peter
McCarthy, Peter
Hoffmann, Peter
Kidd, Stephen
Zilm, Peter
Enterococcus faecalis V583 cell membrane protein expression to alkaline stress
title Enterococcus faecalis V583 cell membrane protein expression to alkaline stress
title_full Enterococcus faecalis V583 cell membrane protein expression to alkaline stress
title_fullStr Enterococcus faecalis V583 cell membrane protein expression to alkaline stress
title_full_unstemmed Enterococcus faecalis V583 cell membrane protein expression to alkaline stress
title_short Enterococcus faecalis V583 cell membrane protein expression to alkaline stress
title_sort enterococcus faecalis v583 cell membrane protein expression to alkaline stress
topic Research Letter
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9491840/
https://www.ncbi.nlm.nih.gov/pubmed/36044998
http://dx.doi.org/10.1093/femsle/fnac082
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