Role of mprF1 and mprF2 in the pathogenicity of Enterococcus faecalis.

<h4>Background</h4>Enterococcus faecalis is one of the leading causes of nosocomial infections. Due to its innate and acquired resistance to most antibiotics, identification of new targets for antimicrobial treatment of E. faecalis is a high priority. The multiple peptide resistance fact...

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Autores principales: Yinyin Bao, Tuerkan Sakinc, Diana Laverde, Dominique Wobser, Abdellah Benachour, Christian Theilacker, Axel Hartke, Johannes Huebner
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spelling oai:doaj.org-article:b2dfb7f56ea746619aa855eba2e8f7562021-11-18T07:15:14ZRole of mprF1 and mprF2 in the pathogenicity of Enterococcus faecalis.1932-620310.1371/journal.pone.0038458https://doaj.org/article/b2dfb7f56ea746619aa855eba2e8f7562012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22723861/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Enterococcus faecalis is one of the leading causes of nosocomial infections. Due to its innate and acquired resistance to most antibiotics, identification of new targets for antimicrobial treatment of E. faecalis is a high priority. The multiple peptide resistance factor MprF, which was first described in Staphylococcus aureus, modifies phosphatidylglycerol with lysin and reduces the negative charge of the membrane, thus increasing resistance to cationic antimicrobial peptides. We studied the effect of mprF in E. faecalis regarding influence on bacterial physiology and virulence.<h4>Results</h4>Two putative mprF paralogs (mprF1 and mprF2) were identified in E. faecalis by BLAST search using the well-described S. aureus gene as a lead. Two deletion mutants in E. faecalis 12030 were created by homologous recombination. Analysis of both mutants by thin-layer chromatography showed that inactivation of mprF2 abolishes the synthesis of three distinct amino-phosphatidylglycerols (PGs). In contrast, deletion of mprF1 did not interfere with the biosynthesis of amino-PG. Inactivation of mprF2 increased susceptibility against several antimicrobial peptides and resulted in a 42% increased biofilm formation compared to wild-type mprF. However, resistance to opsonic killing was increased in the mutant, while virulence in a mouse bacteremia model was unchanged.<h4>Conclusion</h4>Our data suggest that only mprF2 is involved in the aminoacylation of PG in enterococci, and is probably responsible for synthesis of Lys-PG, Ala-PG, and Arg-PG, while mprF1 does not seem to have a role in aminoacylation. As in other Gram-positive pathogens, aminoacylation through MprF2 increases resistance against cationic antimicrobial peptides. Unlike mprF found in other bacteria, mprF2 does not seem to be a major virulence factor in enterococci.Yinyin BaoTuerkan SakincDiana LaverdeDominique WobserAbdellah BenachourChristian TheilackerAxel HartkeJohannes HuebnerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 6, p e38458 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Yinyin Bao
Tuerkan Sakinc
Diana Laverde
Dominique Wobser
Abdellah Benachour
Christian Theilacker
Axel Hartke
Johannes Huebner
Role of mprF1 and mprF2 in the pathogenicity of Enterococcus faecalis.
description <h4>Background</h4>Enterococcus faecalis is one of the leading causes of nosocomial infections. Due to its innate and acquired resistance to most antibiotics, identification of new targets for antimicrobial treatment of E. faecalis is a high priority. The multiple peptide resistance factor MprF, which was first described in Staphylococcus aureus, modifies phosphatidylglycerol with lysin and reduces the negative charge of the membrane, thus increasing resistance to cationic antimicrobial peptides. We studied the effect of mprF in E. faecalis regarding influence on bacterial physiology and virulence.<h4>Results</h4>Two putative mprF paralogs (mprF1 and mprF2) were identified in E. faecalis by BLAST search using the well-described S. aureus gene as a lead. Two deletion mutants in E. faecalis 12030 were created by homologous recombination. Analysis of both mutants by thin-layer chromatography showed that inactivation of mprF2 abolishes the synthesis of three distinct amino-phosphatidylglycerols (PGs). In contrast, deletion of mprF1 did not interfere with the biosynthesis of amino-PG. Inactivation of mprF2 increased susceptibility against several antimicrobial peptides and resulted in a 42% increased biofilm formation compared to wild-type mprF. However, resistance to opsonic killing was increased in the mutant, while virulence in a mouse bacteremia model was unchanged.<h4>Conclusion</h4>Our data suggest that only mprF2 is involved in the aminoacylation of PG in enterococci, and is probably responsible for synthesis of Lys-PG, Ala-PG, and Arg-PG, while mprF1 does not seem to have a role in aminoacylation. As in other Gram-positive pathogens, aminoacylation through MprF2 increases resistance against cationic antimicrobial peptides. Unlike mprF found in other bacteria, mprF2 does not seem to be a major virulence factor in enterococci.
format article
author Yinyin Bao
Tuerkan Sakinc
Diana Laverde
Dominique Wobser
Abdellah Benachour
Christian Theilacker
Axel Hartke
Johannes Huebner
author_facet Yinyin Bao
Tuerkan Sakinc
Diana Laverde
Dominique Wobser
Abdellah Benachour
Christian Theilacker
Axel Hartke
Johannes Huebner
author_sort Yinyin Bao
title Role of mprF1 and mprF2 in the pathogenicity of Enterococcus faecalis.
title_short Role of mprF1 and mprF2 in the pathogenicity of Enterococcus faecalis.
title_full Role of mprF1 and mprF2 in the pathogenicity of Enterococcus faecalis.
title_fullStr Role of mprF1 and mprF2 in the pathogenicity of Enterococcus faecalis.
title_full_unstemmed Role of mprF1 and mprF2 in the pathogenicity of Enterococcus faecalis.
title_sort role of mprf1 and mprf2 in the pathogenicity of enterococcus faecalis.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/b2dfb7f56ea746619aa855eba2e8f756
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