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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

Elizabeth A Clark, Susan Crennell, Abhishek Upadhyay, Alexey V Zozulya, Julia D Mackay, Dmitri I Svergun, Stefan Bagby, and Jean MH van den Elsen

Mol Immunol 48(4):11 (2011) PMID 21055811 PMCID PMC3025320

The structure of the complement-binding domain of Staphylococcus aureus protein Sbi (Sbi-IV) in complex with ligand C3d is presented. The 1.7A 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 @a2 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.

Copyright © 2011 Elsevier Ltd. All rights reserved.

DOI: 10.1016/j.molimm.2010.09.017
Version: za2963e q8zab q8zbc q8zc5 q8zd3 q8zed q8zf5 q8zg9
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