%0 Journal Article %1 Hammel:2007js %A Hammel, Michal %A Sfyroera, Georgia %A Ricklin, Daniel %A Magotti, Paola %A Lambris, John D. %A Geisbrecht, Brian V. %D 2007 %J Nature Immunology %K imported %N 4 %P 430--437 %R 10.1038/ni1450 %T A structural basis for complement inhibition by Staphylococcus aureus. %U http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=17351618&retmode=ref&cmd=prlinks %V 8 %X 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.

@article{Hammel:2007js, 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.}, added-at = {2017-12-08T05:18:19.000+0100}, affiliation = {Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri at Kansas City, Kansas City, Missouri 64110, USA.}, author = {Hammel, Michal and Sfyroera, Georgia and Ricklin, Daniel and Magotti, Paola and Lambris, John D. and Geisbrecht, Brian V.}, biburl = {https://www.bibsonomy.org/bibtex/246962ff81a56f831de13c47dd67cc2f4/lambris}, date-added = {2012-03-27T20:49:01GMT}, date-modified = {2017-12-08T04:17:04GMT}, doi = {10.1038/ni1450}, interhash = {af6b53794c92861c8e354dcecd7c32cb}, intrahash = {46962ff81a56f831de13c47dd67cc2f4}, journal = {Nature Immunology}, keywords = {imported}, language = {English}, month = apr, number = 4, pages = {430--437}, pmid = {17351618}, rating = {0}, timestamp = {2017-12-08T05:18:19.000+0100}, title = {{A structural basis for complement inhibition by Staphylococcus aureus.}}, uri = {\url{papers3://publication/doi/10.1038/ni1450}}, url = {http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=17351618&retmode=ref&cmd=prlinks}, volume = 8, year = 2007 }