TheStreptococcus agalactiaecell wall‐anchored protein PbsP mediates adhesion to and invasion of epithelial cells by exploiting the host vitronectin/αvintegrin axis
| Autor: | Roberta Galbo, Concetta Beninati, Arnaud Firon, Letizia Romeo, Giuseppe Mancuso, Giampiero Pietrocola, Miriam Giardina, Germana Lentini, Isabella Venza, Mario Venza, Angelina Midiri, Pietro Speziale, Carmelo Biondo, Giuseppe Valerio De Gaetano, Giuseppe Teti, Patrick Trieu-Cuot |
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| Přispěvatelé: | Elie Metchnikoff Laboratory, University of Messina, University of Pavia, Centro Neurolesi Bonino Pulejo Messina (IRCCS Messina), Biologie des Bactéries pathogènes à Gram-positif - Biology of Gram-Positive Pathogens, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Scylla Biotech [Messina], Work described here was supported in part by funds granted to Scylla Biotech Srl by the Ministero dell’Università e della Ricerca Scientifica of Italy (Project n.4/13 ex art. 11 D.M. n. 593)., Università degli Studi di Pavia = University of Pavia (UNIPV), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
[SDV]Life Sciences [q-bio] Protein subunit 030106 microbiology Cell Integrin Biology medicine.disease_cause Microbiology Bacterial Adhesion Streptococcus agalactiae MESH: Recombinant Proteins Extracellular matrix 03 medical and health sciences MESH: Cell Wall Bacterial Proteins Protein Domains MESH: Streptococcal Infections Cell Wall Streptococcal Infections medicine Humans Vitronectin MESH: Bacterial Adhesion MESH: Bacterial Proteins Molecular Biology MESH: Humans MESH: Integrin alphaV Epithelial Cells Integrin alphaV MESH: Streptococcus agalactiae MESH: Vitronectin [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Recombinant Proteins Bacterial adhesin [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology medicine.anatomical_structure A549 Cells MESH: Epithelial Cells biology.protein MESH: Protein Domains MESH: Caco-2 Cells Caco-2 Cells MESH: A549 Cells Antibody Molecular Biology vitronectin pbsP GBS Streptococcus |
| Zdroj: | Molecular Microbiology Molecular Microbiology, Wiley, 2018, 110 (1), pp.82-94. ⟨10.1111/mmi.14084⟩ Molecular Microbiology, 2018, 110 (1), pp.82-94. ⟨10.1111/mmi.14084⟩ |
| ISSN: | 1365-2958 0950-382X |
| DOI: | 10.1111/mmi.14084 |
| Popis: | International audience; Binding of microbial pathogens to host vitronectin (Vtn) is a common theme in the pathogenesis of invasive infections. In this study, we characterized the role of Vtn in the invasion of mucosal epithelial cells by Streptococcus agalactiae (i.e. group B streptococcus or GBS), a frequent human pathogen. Moreover, we identified PbsP, a previously described plasminogen-binding protein of GBS, as a dual adhesin that can also interact with human Vtn through its streptococcal surface repeat (SSURE) domains. Deletion of the pbsP gene decreases both bacterial adhesion to Vtn-coated inert surfaces and the ability of GBS to interact with epithelial cells. Bacterial adherence to and invasion of epithelial cells were either inhibited or enhanced by cell pretreatment with, respectively, anti-Vtn antibodies or Vtn, confirming the role of Vtn as a GBS ligand on host cells. Finally, antibodies directed against the integrin αv subunit inhibited Vtn-dependent cell invasion by GBS. Collectively, these results indicate that Vtn acts as a bridge between the SSURE domains of PbsP on the GBS surface and host integrins to promote bacterial invasion of epithelial cells. Therefore, inhibition of interactions between PbsP and extracellular matrix components could represent a viable strategy to prevent colonization and invasive disease by GBS. |
| Databáze: | OpenAIRE |
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