The Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 2

Abstract The commensal bacterium Enterococcus faecalis is a common cause of nosocomial infections worldwide. The increasing prevalence of multi-antibiotic resistant E. faecalis strains reinforces this public health concern. Despite numerous studies highlighting several pathology-related genetic trai...

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Autores principales:	Alexandre Jamet, Rozenn Dervyn, Nicolas Lapaque, Francesca Bugli, Naima G. Perez-Cortez, Hervé M. Blottière, Jean-Claude Twizere, Maurizio Sanguinetti, Brunella Posteraro, Pascale Serror, Emmanuelle Maguin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/369e86fb3cee4f1ba37907fc1fffab45
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spelling	oai:doaj.org-article:369e86fb3cee4f1ba37907fc1fffab452021-12-02T11:52:36ZThe Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 210.1038/s41598-017-04875-32045-2322https://doaj.org/article/369e86fb3cee4f1ba37907fc1fffab452017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04875-3https://doaj.org/toc/2045-2322Abstract The commensal bacterium Enterococcus faecalis is a common cause of nosocomial infections worldwide. The increasing prevalence of multi-antibiotic resistant E. faecalis strains reinforces this public health concern. Despite numerous studies highlighting several pathology-related genetic traits, the molecular mechanisms of E. faecalis virulence remain poorly understood. In this work, we studied 23 bacterial proteins that could be considered as virulence factors or involved in the Enterococcus interaction with the host. We systematically tested their interactions with human proteins using the Human ORFeome library, a set of 12,212 human ORFs, in yeast. Among the thousands of tested interactions, one involving the E. faecalis virulence factor ElrA and the human protein FHL2 was evidenced by yeast two-hybrid and biochemically confirmed. Further molecular characterizations allowed defining an FHL2-interacting domain (FID) of ElrA. Deletion of the FID led to an attenuated in vivo phenotype of the mutated strain clearly indicating that this interaction is likely to contribute to the multifactorial virulence of this opportunistic pathogen. Altogether, our results show that FHL2 is the first host cellular protein directly targeted by an E. faecalis virulence factor and that this interaction is involved in Enterococcus pathogenicity.Alexandre JametRozenn DervynNicolas LapaqueFrancesca BugliNaima G. Perez-CortezHervé M. BlottièreJean-Claude TwizereMaurizio SanguinettiBrunella PosteraroPascale SerrorEmmanuelle MaguinNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alexandre Jamet Rozenn Dervyn Nicolas Lapaque Francesca Bugli Naima G. Perez-Cortez Hervé M. Blottière Jean-Claude Twizere Maurizio Sanguinetti Brunella Posteraro Pascale Serror Emmanuelle Maguin The Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 2
description	Abstract The commensal bacterium Enterococcus faecalis is a common cause of nosocomial infections worldwide. The increasing prevalence of multi-antibiotic resistant E. faecalis strains reinforces this public health concern. Despite numerous studies highlighting several pathology-related genetic traits, the molecular mechanisms of E. faecalis virulence remain poorly understood. In this work, we studied 23 bacterial proteins that could be considered as virulence factors or involved in the Enterococcus interaction with the host. We systematically tested their interactions with human proteins using the Human ORFeome library, a set of 12,212 human ORFs, in yeast. Among the thousands of tested interactions, one involving the E. faecalis virulence factor ElrA and the human protein FHL2 was evidenced by yeast two-hybrid and biochemically confirmed. Further molecular characterizations allowed defining an FHL2-interacting domain (FID) of ElrA. Deletion of the FID led to an attenuated in vivo phenotype of the mutated strain clearly indicating that this interaction is likely to contribute to the multifactorial virulence of this opportunistic pathogen. Altogether, our results show that FHL2 is the first host cellular protein directly targeted by an E. faecalis virulence factor and that this interaction is involved in Enterococcus pathogenicity.
format	article
author	Alexandre Jamet Rozenn Dervyn Nicolas Lapaque Francesca Bugli Naima G. Perez-Cortez Hervé M. Blottière Jean-Claude Twizere Maurizio Sanguinetti Brunella Posteraro Pascale Serror Emmanuelle Maguin
author_facet	Alexandre Jamet Rozenn Dervyn Nicolas Lapaque Francesca Bugli Naima G. Perez-Cortez Hervé M. Blottière Jean-Claude Twizere Maurizio Sanguinetti Brunella Posteraro Pascale Serror Emmanuelle Maguin
author_sort	Alexandre Jamet
title	The Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 2
title_short	The Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 2
title_full	The Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 2
title_fullStr	The Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 2
title_full_unstemmed	The Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 2
title_sort	enterococcus faecalis virulence factor elra interacts with the human four-and-a-half lim domains protein 2
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/369e86fb3cee4f1ba37907fc1fffab45
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The Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 2

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