ArticleScientific reports2017
The Staphylococcus aureus extracellular matrix protein (Emp) has a fibrous structure and binds to different extracellular matrices.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.
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21 citing papers in PubMed, 34 citations in OpenAlex.
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- Bacterial adhesion strategies and countermeasures in urinary tract infection.Nature microbiology · 2025Review
- An Investigation of Virulence Genes ofAnimals : an open access journal from MDPI · 2024Article
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- Identification of virulence-associated factors in Vibrio parahaemolyticus with special reference to moonlighting protein: a secretomics study.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- Clonal Diversity, Antibiotic Resistance, and Virulence Factor Prevalence of Community AssociatedPathogens (Basel, Switzerland) · 2023Article
- Resistance, Tolerance, Virulence and Bacterial Pathogen Fitness-Current State and Envisioned Solutions for the Near Future.Pathogens (Basel, Switzerland) · 2023Review
- Clinical Impact ofAntibiotics (Basel, Switzerland) · 2023Review
- The Small RNA Teg41 Is a Pleiotropic Regulator of Virulence in Staphylococcus aureus.Infection and immunity · 2022Article
- The EcpD Tip Adhesin of theInternational journal of molecular sciences · 2022Article
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- Spatially Targeted Proteomics of the Host-Pathogen Interface during Staphylococcal Abscess Formation.ACS infectious diseases · 2021Article
- Collagen Binding Proteins of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- Searching for the Secret of Stickiness: How Biofilms Adhere to Surfaces.Frontiers in microbiology · 2021Review
- Article
Corrections and comments
- Erratum issued
Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The extracellular matrix protein Emp of Staphylococcus aureus is a secreted adhesin that mediates interactions between the bacterial surface and extracellular host structures. However, its structure and role in staphylococcal pathogenesis remain unknown. Using multidisciplinary approaches, including circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy, transmission electron (TEM) and immunogold transmission electron microscopy, functional ELISA assays and in silico techniques, we characterized the Emp protein. We demonstrated that Emp and its truncated forms bind to suprastructures in human skin, cartilage or bone, among which binding activity seems to be higher for skin compounds. The binding domain is located in the C-terminal part of the protein. CD spectroscopy revealed high contents of β-sheets (39.58%) and natively disordered structures (41.2%), and TEM suggested a fibrous structure consisting of Emp polymers. The N-terminus seems to be essential for polymerization. Due to the uncommonly high histidine content, we suggest that Emp represents a novel type of histidine-rich protein sharing structural similarities to leucine-rich repeats proteins as predicted by the I-TASSER algorithm. These new findings suggest a role of Emp in infections of deeper tissue and open new possibilities for the development of novel therapeutic strategies.
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