A structural basis for complement inhibition by Staphylococcus aureus.
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Hammel M, Sfyroera G, Ricklin D, Magotti P, Lambris JD, Geisbrecht BV
A structural basis for complement inhibition by Staphylococcus aureus.
Nat Immunol. 2007 Apr;8(4):430-7. Epub 2007 Mar 11.
- PubMed ID
- 17351618 [ View in PubMed]
- Abstract
To provide insight into bacterial suppression of complement-mediated immunity, we present here structures of a bacterial complement inhibitory protein, both free and bound to its complement target. The 1.25-A structure of the complement component C3-inhibitory domain of Staphylococcus aureus extracellular fibrinogen-binding protein (Efb-C) demonstrated a helical motif involved in complement regulation, whereas the 2.2-A structure of Efb-C bound to the C3d domain of human C3 allowed insight into the recognition of complement proteins by invading pathogens. Our structure-function studies provided evidence for a previously unrecognized mode of complement inhibition whereby Efb-C binds to native C3 and alters the solution conformation of C3 in a way that renders it unable to participate in successful 'downstream' activation of the complement response.