ArticleScientific reports2016
Group A Streptococcus exploits human plasminogen for bacterial translocation across epithelial barrier via tricellular tight junctions.
Article in Scientific reports, 2016. 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 26 papers.
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Who cites it
26 citing papers in PubMed, 52 citations in OpenAlex.
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- Characterization of a novelmBio · 2025Article
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- The Basic Requirement of Tight Junction Proteins in Blood-Brain Barrier Function and Their Role in Pathologies.International journal of molecular sciences · 2024Review
- Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024Review
- Palmitoylation of proteolipid protein M6 promotes tricellular junction assembly in epithelia of Drosophila.Journal of cell science · 2024Article
- The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into Plasmin.Microorganisms · 2023Article
- MPL36, a major plasminogen (PLG) receptor in pathogenic Leptospira, has an essential role during infection.PLoS pathogens · 2023Article
- The Recruitment and Activation of Plasminogen by Bacteria-The Involvement in Chronic Infection Development.International journal of molecular sciences · 2023Review
- Group BScience advances · 2022Article
- Micronutrient Improvement of Epithelial Barrier Function in Various Disease States: A Case for Adjuvant Therapy.International journal of molecular sciences · 2022Review
- Interaction of helminth parasites with the haemostatic system of their vertebrate hosts: a scoping review.Parasite (Paris, France) · 2022Article
- GP96 Drives Exacerbation of Secondary Bacterial Pneumonia following Influenza A Virus Infection.mBio · 2021Article
- Intracellular Group AmBio · 2021Article
- Group AFrontiers in cardiovascular medicine · 2021Article
- The M Protein of Streptococcus pyogenes Strain AP53 Retains Cell Surface Functional Plasminogen Binding after Inactivation of the Sortase A Gene.Journal of bacteriology · 2020Article
- Host Pathways of Hemostasis that Regulate Group A Streptococcus pyogenes Pathogenicity.Current drug targets · 2020Article
- Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcus pyogenes.Journal of structural biology · 2019Article
- Variations in the secondary structures of PAM proteins influence their binding affinities to human plasminogen.Journal of structural biology · 2019Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Group A Streptococcus (GAS) is a human-specific pathogen responsible for local suppurative and life-threatening invasive systemic diseases. Interaction of GAS with human plasminogen (PLG) is a salient characteristic for promoting their systemic dissemination. In the present study, a serotype M28 strain was found predominantly localized in tricellular tight junctions of epithelial cells cultured in the presence of PLG. Several lines of evidence indicated that interaction of PLG with tricellulin, a major component of tricellular tight junctions, is crucial for bacterial localization. A site-directed mutagenesis approach revealed that lysine residues at positions 217 and 252 within the extracellular loop of tricellulin play important roles in PLG-binding activity. Additionally, we demonstrated that PLG functions as a molecular bridge between tricellulin and streptococcal surface enolase (SEN). The wild type strain efficiently translocated across the epithelial monolayer, accompanied by cleavage of transmembrane junctional proteins. In contrast, amino acid substitutions in the PLG-binding motif of SEN markedly compromised those activities. Notably, the interaction of PLG with SEN was dependent on PLG species specificity, which influenced the efficiency of bacterial penetration. Our findings provide insight into the mechanism by which GAS exploits host PLG for acceleration of bacterial invasion into deeper tissues via tricellular tight junctions.
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