ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structural and functional analysis of an anchorless fibronectin-binding protein FBPS from Gram-positive bacterium Streptococcus suis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 34 citations in OpenAlex.
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- Evaluation of the effect of host-derived Latilactobacillus sakei MG6 on the physiological health and intestinal homeostasis in turbot (Scophthalmus maximus L.).Scientific reports · 2026Article
- Serovar-Dependent Gene Regulation and Antimicrobial Tolerance inAntibiotics (Basel, Switzerland) · 2025Article
- FabG moonlights as an extracellular adhesin mediates cytoadhesion of Streptococcus suis via interaction with plasminogen.BMC microbiology · 2025Article
- Current prevalence and therapeutic strategies for porcineApplied and environmental microbiology · 2025Review
- Effects of AI-2 quorum sensing related luxS gene on Streptococcus suis formatting monosaccharide metabolism-dependent biofilm.Archives of microbiology · 2024Article
- Ribosome-associated quality-control mechanisms from bacteria to humans.Molecular cell · 2022Review
- Binding of Plasminogen toFrontiers in microbiology · 2021Article
- Pathogenesis ofVirulence · 2020Article
- Longitudinal Metatranscriptomic Analysis of a Meat Spoilage Microbiome Detects Abundant Continued Fermentation and Environmental Stress Responses during Shelf Life and Beyond.Applied and environmental microbiology · 2020Article
- Functional Analysis of a Fibronectin Binding Protein of Streptococcus parasanguinis FW213.Current microbiology · 2020Article
- Proteomic and Metabolomic Analyses Provide Insights into the Mechanism on Arginine Metabolism Regulated by tRNA Modification Enzymes GidA and MnmE ofFrontiers in cellular and infection microbiology · 2020Article
- Crystal structure of the N-terminal domain of the fibronectin-binding protein PavA from Streptococcus pneumoniae.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Article
- Molecular Basis of a Protective/Neutralizing Monoclonal Antibody Targeting Envelope Proteins of both Tick-Borne Encephalitis Virus and Louping Ill Virus.Journal of virology · 2019Article
- Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.Frontiers in microbiology · 2018Review
- The non-conserved region of MRP is involved in the virulence of Streptococcus suis serotype 2.Virulence · 2017Article
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The anchorless fibronectin-binding proteins (FnBPs) are a group of important virulence factors for which the structures are not available and the functions are not well defined. In this study we performed comprehensive studies on a prototypic member of this group: the fibronectin-/fibrinogen-binding protein from Streptococcus suis (FBPS). The structures of the N- and C-terminal halves (FBPS-N and FBPS-C), which together cover the full-length protein in sequence, were solved at a resolution of 2.1 and 2.6 Å, respectively, and each was found to be composed of two domains with unique folds. Furthermore, we have elucidated the organization of these domains by small-angle X-ray scattering. We further showed that the fibronectin-binding site is located in FBPS-C and that FBPS promotes the adherence of S suis to host cells by attaching the bacteria via FBPS-N. Finally, we demonstrated that FBPS functions both as an adhesin, promoting S suis attachment to host cells, and as a bacterial factor, activating signaling pathways via β1 integrin receptors to induce chemokine production.
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