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dc.contributor.authorGEOGHEGAN, JOANen
dc.contributor.authorFOSTER, TIMOTHYen
dc.date.accessioned2014-12-01T11:13:16Z
dc.date.available2014-12-01T11:13:16Z
dc.date.issued2013en
dc.date.submitted2013en
dc.identifier.citationHair PS, Foley CK, Krishna NK, Nyalwidhe JO, Geoghegan JA, Foster TJ, Cunnion KM, Complement regulator C4BP binds to Staphylococcus aureus surface proteins SdrE and Bbp inhibiting bacterial opsonization and killing., Results in immunology, 3, 2013, 114-21en
dc.identifier.otherYen
dc.identifier.urihttp://hdl.handle.net/2262/72310
dc.descriptionPUBLISHEDen
dc.description.abstractStaphylococcus aureus is a premier human pathogen and the most common cause of osteoarticular, wound, and implanted device infections. We recently demonstrated S. aureus efficiently binds the classical complement regulator C4b-binding protein (C4BP) inhibiting antibody-initiated complement-mediated opsonization. Here we identify S. aureus surface protein SdrE as a C4BP-binding protein. Recombinant SdrE and recombinant bone sialoprotein-binding protein (Bbp), an allelic variant of SdrE, both efficiently bound to C4BP in heat-inactivated human serum. We previously described SdrE as binding alternative pathway regulator factor H. Recombinant SdrE and Bbp efficiently bound C4BP and factor H in serum without apparent interference. Gain of function studies utilizing Lactococcus lactis clones expressing SdrE or Bbp increased serum C4BP and factor H binding, compared with empty-vector control (WT) approximately 2-fold. Correspondingly, classical pathway-mediated C3-fragment opsonization and bacterial killing by human neutrophils decreased by half for L. lactis clones expressing SdrE or Bbp compared with WT. In summary, we identify SdrE and allelic variant Bbp as S. aureus surface proteins that bind the complement regulator C4BP inhibiting classical pathway-mediated bacterial opsonization and killing.en
dc.format.extent114-21en
dc.language.isoenen
dc.relation.ispartofseriesResults in immunologyen
dc.relation.ispartofseries3en
dc.rightsYen
dc.subjectStaphylococcus aureusen
dc.subjectSdrEen
dc.subjectOpsonophagocytosisen
dc.subjectComplementen
dc.subjectC4BPen
dc.titleComplement regulator C4BP binds to Staphylococcus aureus surface proteins SdrE and Bbp inhibiting bacterial opsonization and killing.en
dc.typeJournal Articleen
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/geoghejoen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/tfosteren
dc.identifier.rssinternalid92469en
dc.identifier.doihttp://dx.doi.org/10.1016/j.rinim.2013.10.004en
dc.rights.ecaccessrightsopenAccess
dc.subject.TCDThemeImmunology, Inflammation & Infectionen
dc.subject.TCDTagIMMUNOLOGYen
dc.subject.TCDTagInnate immunologyen
dc.subject.TCDTagMicrobiologyen
dc.subject.TCDTagMolecular Biologyen
dc.subject.TCDTagstaphylococcusen


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