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Abstract
The structure of the complement-binding domain of Staphylococcus aureus protein Sbi (Sbi-IV) in complex with ligand C3d is presented. The 1.7 angstrom 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 alpha 2 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.
Original language | English |
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Pages (from-to) | 452-462 |
Journal | Molecular Immunology |
Volume | 48 |
Issue number | 4 |
DOIs | |
Publication status | Published - Jan 2011 |
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Dive into the research topics of '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'. Together they form a unique fingerprint.Projects
- 1 Finished
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NOVEL COMPLEMENT INHIBITING THERAPEUTIC BASED ON STAPHYLOCOC CUS AUREUS PROTEIN SBI
Van Den Elsen, J. (PI) & Bagby, S. (CoI)
Biotechnology and Biological Sciences Research Council
1/11/07 → 28/02/09
Project: Research council