ArticleJournal of bacteriology2015
The identification and functional characterization of WxL proteins from Enterococcus faecium reveal surface proteins involved in extracellular matrix interactions.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 39 citations in OpenAlex.
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- Phage P100 resistance in clinical and foodborneCurrent research in microbial sciences · 2026Article
- A conserved sRNA regulates mucin adhesion and gut colonization across the Enterococcaceae.bioRxiv : the preprint server for biology · 2025Article
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- Heterologous expression of the Oenococcus oeni two-component signal transduction response regulator in the Lactiplantibacillus plantarum WCFS1 strain enhances acid stress tolerance.BMC microbiology · 2024Article
- Review
- 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
- An RNA modification enzyme directly senses reactive oxygen species for translational regulation in Enterococcus faecalis.Nature communications · 2023Article
- Bioinformatic analysis of WxL domain proteins.Saudi journal of biological sciences · 2023Article
- Evidence of pediatric sepsis caused by a drug resistantEmerging microbes & infections · 2022Article
- Identification of WxL and S-Layer Proteins fromInternational journal of molecular sciences · 2022Article
- Genomic Insights ofFrontiers in microbiology · 2022Article
- Microdiversity ofEmerging microbes & infections · 2021Article
- Butanol Tolerance ofGenes · 2021Article
- Development and Characterization of High-ThroughputFrontiers in cellular and infection microbiology · 2021Article
- Review
- A deletion in the RD105 region confers resistance to multiple drugs in Mycobacterium tuberculosis.BMC biology · 2019Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
The WxL domain recently has been identified as a novel cell wall binding domain found in numerous predicted proteins within multiple Gram-positive bacterial species. However, little is known about the function of proteins containing this novel domain. Here, we identify and characterize 6 Enterococcus faecium proteins containing the WxL domain which, by reverse transcription-PCR (RT-PCR) and genomic analyses, are located in three similarly organized operons, deemed WxL loci A, B, and C. Western blotting, electron microscopy, and enzyme-linked immunosorbent assays (ELISAs) determined that genes of WxL loci A and C encode antigenic, cell surface proteins exposed at higher levels in clinical isolates than in commensal isolates. Secondary structural analyses of locus A recombinant WxL domain-containing proteins found they are rich in β-sheet structure and disordered segments. Using Biacore analyses, we discovered that recombinant WxL proteins from locus A bind human extracellular matrix proteins, specifically type I collagen and fibronectin. Proteins encoded by locus A also were found to bind to each other, suggesting a novel cell surface complex. Furthermore, bile salt survival assays and animal models using a mutant from which all three WxL loci were deleted revealed the involvement of WxL operons in bile salt stress and endocarditis pathogenesis. In summary, these studies extend our understanding of proteins containing the WxL domain and their potential impact on colonization and virulence in E. faecium and possibly other Gram-positive bacterial species.
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Registered trials
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