ArticlePLoS pathogens2008
The Staphylococcus aureus protein Sbi acts as a complement inhibitor and forms a tripartite complex with host complement Factor H and C3b.
Article in PLoS pathogens, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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78 citing papers in PubMed, 135 citations in OpenAlex.
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- The human factor H protein family - an update.Frontiers in immunology · 2024Review
- PathogenicInfection and immunity · 2022Article
- Novel method for detecting complement C3 deposition on Staphylococcus aureus.Scientific reports · 2022Article
- Group BJournal of immunology (Baltimore, Md. : 1950) · 2022Article
- The Protease SplB of Staphylococcus aureus Targets Host Complement Components and Inhibits Complement-Mediated Bacterial Opsonophagocytosis.Journal of bacteriology · 2022Article
- A General Map of Transcriptional Expression of Virulence, Metabolism, and Biofilm Formation Adaptive Changes ofFrontiers in microbiology · 2022Article
- CipA mediates complement resistance ofFrontiers in immunology · 2022Article
- Staphylococcal Complement Evasion Protein Sbi Stabilises C3d Dimers by Inducing an N-Terminal Helix Swap.Frontiers in immunology · 2022Article
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- Complement Inactivation Strategy ofInternational journal of molecular sciences · 2021Article
- MBOVPG45_0375 Encodes an IgG-Binding Protein and MBOVPG45_0376 Encodes an IgG-Cleaving Protein inFrontiers in veterinary science · 2021Article
- Hijacking Factor H for Complement Immune Evasion.Frontiers in immunology · 2021Review
- Complement-Independent Modulation of Influenza A Virus Infection by Factor H.Frontiers in immunology · 2020Article
- The Role of Macrophages inFrontiers in immunology · 2020Review
18 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Gram-positive bacterium Staphylococcus aureus, similar to other pathogens, binds human complement regulators Factor H and Factor H related protein 1 (FHR-1) from human serum. Here we identify the secreted protein Sbi (Staphylococcus aureus binder of IgG) as a ligand that interacts with Factor H by a-to our knowledge-new type of interaction. Factor H binds to Sbi in combination with C3b or C3d, and forms tripartite SbiratioC3ratioFactor H complexes. Apparently, the type of C3 influences the stability of the complex; surface plasmon resonance studies revealed a higher stability of C3d complexed to Sbi, as compared to C3b or C3. As part of this tripartite complex, Factor H is functionally active and displays complement regulatory activity. Sbi, by recruiting Factor H and C3b, acts as a potent complement inhibitor, and inhibits alternative pathway-mediated lyses of rabbit erythrocytes by human serum and sera of other species. Thus, Sbi is a multifunctional bacterial protein, which binds host complement components Factor H and C3 as well as IgG and beta(2)-glycoprotein I and interferes with innate immune recognition.
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