ArticleMolecular immunology2011
A structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d.
Article in Molecular immunology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Article
- Novel method for detecting complement C3 deposition on Staphylococcus aureus.Scientific reports · 2022Article
- Complement component C3: A structural perspective and potential therapeutic implications.Seminars in immunology · 2022Review
- Staphylococcal Complement Evasion Protein Sbi Stabilises C3d Dimers by Inducing an N-Terminal Helix Swap.Frontiers in immunology · 2022Article
- Insights Into the Structure-Function Relationships of Dimeric C3d Fragments.Frontiers in immunology · 2021Article
- Neuropilin-1 Acts as a Receptor for Complement Split Products.Frontiers in immunology · 2019Article
- Utilization of Staphylococcal Immune Evasion Protein Sbi as a Novel Vaccine Adjuvant.Frontiers in immunology · 2018Article
- Importance of B Lymphocytes and the IgG-Binding Protein Sbi in Staphylococcus aureus Skin Infection.Pathogens (Basel, Switzerland) · 2016Article
- Molecular analysis of the interaction between staphylococcal virulence factor Sbi-IV and complement C3d.Biophysical journal · 2014Article
- Regulation of humoral immunity by complement.Immunity · 2012Review
- The two sides of complement C3d: evolution of electrostatics in a link between innate and adaptive immunity.PLoS computational biology · 2012Article
- Staphylococcus aureus proteins Sbi and Efb recruit human plasmin to degrade complement C3 and C3b.PloS one · 2012Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The structure of the complement-binding domain of Staphylococcus aureus protein Sbi (Sbi-IV) in complex with ligand C3d is presented. The 1.7Å resolution structure reveals the molecular details of the recognition of thioester-containing fragment C3d of the central complement component C3, involving interactions between residues of Sbi-IV helix α2 and the acidic concave surface of C3d. The complex provides a structural basis for the binding preference of Sbi for native C3 over C3b and explains how Sbi-IV inhibits the interaction between C3d and complement receptor 2. A second C3d binding site on Sbi-IV is identified in the crystal structure that is not observed in related S. aureus C3 inhibitors Efb-C and Ehp. This binding mode perhaps hints as to how Sbi-IV, as part of Sbi, forms a C3b-Sbi adduct and causes futile consumption of C3, an extraordinary aspect of Sbi function that is not shared by any other known Staphylococcal complement inhibitor.
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