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

Reference:

Clark, E. A., Crennell, S., Upadhyay, A., Zozulya, A. V., Mackay, J. D., Svergun, D. I., Bagby, S. and van den Elsen, J. M. H., 2011. 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. Molecular Immunology, 48 (4), pp. 452-462.

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Official URL:

http://dx.doi.org/10.1016/j.molimm.2010.09.017

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.

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