ArticleThe Journal of biological chemistry2012
The extracellular protein factor Epf from Streptococcus pyogenes is a cell surface adhesin that binds to cells through an N-terminal domain containing a carbohydrate-binding module.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Streptolysin O accelerates the conversion of plasminogen to plasmin.Nature communications · 2024Article
- Review
- A novel sialic acid-binding adhesin present in multiple species contributes to the pathogenesis of Infective endocarditis.PLoS pathogens · 2021Article
- The N-terminal domain of the R28 protein promotesThe Journal of biological chemistry · 2018Article
- Canada-Wide Epidemic ofOpen forum infectious diseases · 2018Article
- Port d'Entrée for Respiratory Infections - Does the Influenza A Virus Pave the Way for Bacteria?Frontiers in microbiology · 2017Review
- Streptococcus pyogenes Escapes Killing from Extracellular Histones through Plasminogen Binding and Activation by Streptokinase.Journal of innate immunity · 2016Article
- In Vivo Tracking of Streptococcal Infections of Subcutaneous Origin in a Murine Model.Molecular imaging and biology · 2015Article
- Streptococcus pyogenes triggers activation of the human contact system by streptokinase.Infection and immunity · 2015Article
- Structural basis of Staphylococcus epidermidis biofilm formation: mechanisms and molecular interactions.Frontiers in cellular and infection microbiology · 2015Review
- Rethinking Molecular Mimicry in Rheumatic Heart Disease and Autoimmune Myocarditis: Laminin, Collagen IV, CAR, and B1AR as Initial Targets of Disease.Frontiers in pediatrics · 2014Article
- Severe soft tissue infection caused by a non-beta-hemolytic Streptococcus pyogenes strain harboring a premature stop mutation in the sagC gene.Journal of clinical microbiology · 2013Article
- Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system.Frontiers in cellular and infection microbiology · 2013Review
- Structural and functional analysis of the N-terminal domain of the Streptococcus gordonii adhesin Sgo0707.PloS one · 2013Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus pyogenes is an exclusively human pathogen. Streptococcal attachment to and entry into epithelial cells is a prerequisite for a successful infection of the human host and requires adhesins. Here, we demonstrate that the multidomain protein Epf from S. pyogenes serotype M49 is a streptococcal adhesin. An epf-deficient mutant showed significantly decreased adhesion to and internalization into human keratinocytes. Cell adhesion is mediated by the N-terminal domain of Epf (EpfN) and increased by the human plasma protein plasminogen. The crystal structure of EpfN, solved at 1.6 Å resolution, shows that it consists of two subdomains: a carbohydrate-binding module and a fibronectin type III domain. Both fold types commonly participate in ligand receptor and protein-protein interactions. EpfN is followed by 18 repeats of a domain classified as DUF1542 (domain of unknown function 1542) and a C-terminal cell wall sorting signal. The DUF1542 repeats are not involved in adhesion, but biophysical studies show they are predominantly α-helical and form a fiber-like stalk of tandem DUF1542 domains. Epf thus conforms with the widespread family of adhesins known as MSCRAMMs (microbial surface components recognizing adhesive matrix molecules), in which a cell wall-attached stalk enables long range interactions via its adhesive N-terminal domain.
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