Article abstract
Nature Immunology 8, 430 - 437 (2007)
Published online: 11 March 2007 | doi:10.1038/ni1450
A structural basis for complement inhibition by Staphylococcus aureus
Michal Hammel1,3,4, Georgia Sfyroera2,4, Daniel Ricklin2, Paola Magotti2, John D Lambris2 & Brian V Geisbrecht1
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-Å 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-Å 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.
- Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri at Kansas City, Kansas City, Missouri 64110, USA.
- Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
- Present address: Advanced Light Source, Lawrence Berkeley Laboratory, Berkeley, California 94720, USA.
- These authors contributed equally to this work.
Correspondence to: Brian V Geisbrecht1 e-mail: geisbrechtB@umkc.edu
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