ArticleScientific reports2017
The Enterococcus faecalis virulence factor ElrA interacts with the human Four-and-a-Half LIM Domains Protein 2.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 17 citations in OpenAlex.
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- Current Knowledge of Enterococcal Endocarditis: A Disease Lurking in Plain Sight of Health Providers.Pathogens (Basel, Switzerland) · 2024Review
- Enterococcal-host interactions in the gastrointestinal tract and beyond.FEMS microbes · 2024Review
- DUF916 and DUF3324 in the WxL protein cluster bind to WxL and link bacterial and host surfaces.Protein science : a publication of the Protein Society · 2023Article
- The Role of Platelets in Infective Endocarditis.International journal of molecular sciences · 2023Review
- Bioinformatic analysis of WxL domain proteins.Saudi journal of biological sciences · 2023Article
- Virulence Factors in Colorectal Cancer Metagenomes and Association of Microbial Siderophores with Advanced Stages.Microorganisms · 2022Article
- Enterococcal Endocarditis: Hiding in Plain Sight.Frontiers in cellular and infection microbiology · 2021Review
- Exploration of the role of the virulence factor ElrA during Enterococcus faecalis cell infection.Scientific reports · 2018Article
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Authors and funding
11 authors at 4 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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