دورية أكاديمية
أعرض في EDS

The serine-rich repeat glycoprotein Srr2 mediates Streptococcus agalactiae interaction with host fibronectin.

التفاصيل البيبلوغرافية
العنوان: The serine-rich repeat glycoprotein Srr2 mediates Streptococcus agalactiae interaction with host fibronectin.
المؤلفون: Pellegrini A; Department of Molecular Medicine, University of Pavia, Pavia, Italy., Motta C; Department of Molecular Medicine, University of Pavia, Pavia, Italy., Bellan Menegussi E; Department of Molecular Medicine, University of Pavia, Pavia, Italy., Pierangelini A; Department of Pharmaceutical and Pharmacological Sciences, University of Padua, Padua, Italy., Viglio S; Department of Molecular Medicine, University of Pavia, Pavia, Italy., Coppolino F; Department of Human Pathology and Medicine, University of Messina, Messina, Italy., Beninati C; Department of Human Pathology and Medicine, University of Messina, Messina, Italy., De Filippis V; Department of Pharmaceutical and Pharmacological Sciences, University of Padua, Padua, Italy., Barbieri G; Department of Biology and Biotechnology 'Lazzaro Spallanzani', University of Pavia, Pavia, Italy. giulia.barbieri@unipv.it., Pietrocola G; Department of Molecular Medicine, University of Pavia, Pavia, Italy. giampiero.pietrocola@unipv.it.
المصدر: BMC microbiology [BMC Microbiol] 2024 Jun 22; Vol. 24 (1), pp. 221. Date of Electronic Publication: 2024 Jun 22.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: BioMed Central Country of Publication: England NLM ID: 100966981 Publication Model: Electronic Cited Medium: Internet ISSN: 1471-2180 (Electronic) Linking ISSN: 14712180 NLM ISO Abbreviation: BMC Microbiol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: London : BioMed Central, [2001-
مواضيع طبية MeSH: Streptococcus agalactiae*/genetics , Streptococcus agalactiae*/metabolism , Streptococcus agalactiae*/pathogenicity , Fibronectins*/metabolism , Adhesins, Bacterial*/metabolism , Adhesins, Bacterial*/genetics , Bacterial Adhesion* , Protein Binding*, Humans ; Fibrinogen/metabolism ; Fibrinogen/genetics ; Epithelial Cells/microbiology ; Female ; Streptococcal Infections/microbiology ; Virulence Factors/metabolism ; Virulence Factors/genetics
مستخلص: Background: Group B Streptococcus (GBS) is a commensal of healthy adults and an important pathogen in newborns, the elderly and immunocompromised individuals. GBS displays several virulence factors that promote colonisation and host infection, including the ST-17 strain-specific adhesin Srr2, previously characterised for its binding to fibrinogen. Another common target for bacterial adhesins and for host colonization is fibronectin, a multi-domain glycoprotein found ubiquitously in body fluids, in the extracellular matrix and on the surface of cells.
Results: In this study, fibronectin was identified as a novel ligand for the Srr2 adhesin of GBS. A derivative of the ST-17 strain BM110 overexpressing the srr2 gene showed an increased ability to bind fibrinogen and fibronectin, compared to the isogenic wild-type strain. Conversely, the deletion of srr2 impaired bacterial adhesion to both ligands. ELISA assays and surface plasmon resonance studies using the recombinant binding region (BR) form of Srr2 confirmed a direct interaction with fibronectin with an estimated Kd of 92 nM. Srr2-BR variants defective in fibrinogen binding also exhibited no interaction with fibronectin, suggesting that Srr2 binds this ligand through the dock-lock-latch mechanism, previously described for fibrinogen binding. The fibronectin site responsible for recombinant Srr2-BR binding was identified and localised in the central cell-binding domain of the protein. Finally, in the presence of fibronectin, the ability of a Δsrr2 mutant to adhere to human cervico-vaginal epithelial cells was significantly lower than that of the wild-type strain.
Conclusion: By combining genetic and biochemical approaches, we demonstrate a new role for Srr2, namely interacting with fibronectin. We characterised the molecular mechanism of this interaction and demonstrated that it plays a role in promoting the adhesion of GBS to human cervico-vaginal epithelial cells, further substantiating the role of Srr2 as a factor responsible for the hypervirulence of GBS ST-17 strains. The discovery of the previously undescribed interaction between Srr2 and fibronectin establishes this adhesin as a key factor for GBS colonisation of host tissues.
(© 2024. The Author(s).)
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معلومات مُعتمدة: BPiTA n. 52012 CaRiPaRo Foundation Excellence Research Project; MUR-PRIN-2022 n. 2022ZSA2JP Italian Ministry for Universities and Research; PE00000007, INF-ACT EU funding within the Next-generation EU-MUR PNRR Extended Partnership initiative on Emerging Infectious Diseases
فهرسة مساهمة: Keywords: Bacterial adhesins; DLL binding mechanism; Fibronectin; Host-pathogen interaction; Srr2 adhesin; Streptococcus agalactiae
المشرفين على المادة: 0 (Fibronectins)
0 (Adhesins, Bacterial)
9001-32-5 (Fibrinogen)
0 (Virulence Factors)
تواريخ الأحداث: Date Created: 20240622 Date Completed: 20240622 Latest Revision: 20240711
رمز التحديث: 20240711
مُعرف محوري في PubMed: PMC11193222
DOI: 10.1186/s12866-024-03374-6
PMID: 38909237
قاعدة البيانات: MEDLINE
الوصف
تدمد:1471-2180
DOI:10.1186/s12866-024-03374-6