ArticleInfection and immunity2015
The fibronectin-binding protein Fnm contributes to adherence to extracellular matrix components and virulence of Enterococcus faecium.
Article in Infection and immunity, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Chemoproteomic profiling of adaptive ATP-binding protein activity inFEMS microbes · 2026Article
- Assessment of Factors Contributing to Infection Severity and High Levels of Drug Resistance in Clinical Enterococcus Isolates.Journal of clinical laboratory analysis · 2025Article
- Enterococcus faecium: evolution, adaptation, pathogenesis and emerging therapeutics.Nature reviews. Microbiology · 2024Review
- Genomic context as well as sequence of bothmBio · 2024Article
- Activity-based protein profiling of serine hydrolases and penicillin-binding proteins inFEMS microbes · 2024Article
- Evaluation of novel compounds as anti-bacterial or anti-virulence agents.Frontiers in cellular and infection microbiology · 2024Review
- Enterococcal-host interactions in the gastrointestinal tract and beyond.FEMS microbes · 2024Review
- The population structure of vancomycin-resistant and -susceptibleMicrobial genomics · 2023Article
- NADH oxidase of Mycoplasma synoviae is a potential diagnostic antigen, plasminogen/fibronectin binding protein and a putative adhesin.BMC veterinary research · 2022Article
- Features and Colonization Strategies ofFrontiers in microbiology · 2022Article
- Review
- Article
- Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.Frontiers in microbiology · 2018Review
- Fibrinogen and mucin binding activity of EF0737, a novel protein ofIranian journal of microbiology · 2017Article
- Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The interaction between bacteria and fibronectin is believed to play an important role in the pathogenicity of clinically important Gram-positive cocci. In the present study, we identified a gene encoding a predicted fibronectin-binding protein of Enterococcus faecium (fnm), a homologue of Streptococcus pneumoniae pavA, in the genomes of E. faecium strain TX82 and all other sequenced E. faecium isolates. Full-length recombinant Fnm from strain TX82 bound to immobilized fibronectin in a concentration-dependent manner and also appeared to bind collagen type V and laminin, but not other proteins, such as transferrin, heparin, bovine serum albumin, mucin, or collagen IV. We demonstrated that the N-terminal fragment of Fnm is required for full fibronectin binding, since truncation of this region caused a 2.4-fold decrease (P < 0.05) in the adhesion of E. faecium TX82 to fibronectin. Deletion of fnm resulted in a significant reduction (P < 0.001) in the ability of the mutant, TX6128, to bind fibronectin relative to that of the wild-type strain; in situ reconstitution of fnm in the deletion mutant strain restored adherence. In addition, the Δfnm mutant was highly attenuated relative to TX82 (P ≤ 0.0001) in a mixed-inoculum rat endocarditis model. Taken together, these results demonstrate that Fnm affects the adherence of E. faecium to fibronectin and is important in the pathogenesis of experimental endocarditis.
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