expresses surface proteins that closely resemble those from

Joan A. Geoghegan , Emma J. Smith , Pietro Speziale , Timothy J. Foster

is a commensal of dogs that is implicated in the pathogenesis of canine pyoderma. This study aimed to determine if expresses surface proteins resembling those from and to characterise them. strain 326 was shown to adhere strongly to purified fibrinogen, fibronectin and cytokeratin 10. It adhered to the α-chain of fibrinogen which, along with binding to cytokeratin 10, is the hallmark of clumping factor B of , a surface protein that is in part responsible for colonization of the human nares. Ligand-affinity blotting with cell-wall extracts demonstrated that 326 expressed a cell-wall anchored fibronectin binding protein which recognised the N-terminal 29 kDa fragment. The ability to bind fibronectin is an important attribute of pathogenic and is associated with the ability of to colonize skin of human atopic dermatitis patients. genomic DNA was probed with labelled DNA amplified from the serine-aspartate repeat encoding region of of . This probe hybridised to a single I fragment of DNA. In the cell wall extract of 326 a 180 kDa protein was discovered which bound to fibrinogen by ligand-affinity blotting and reacted in a Western blot with antibodies raised against the serine-aspartate repeat region of ClfA and the B-repeats of SdrD of . It is proposed that this is an Sdr protein with B-repeats that has an A domain that binds to fibrinogen. Whether it is the same protein that binds cytokeratin 10 is not clear.

Mots clés: Medicine

Joan A. Geoghegan, Emma J. Smith, Pietro Speziale, Timothy J. Foster. expresses surface proteins that closely resemble those from. Veterinary Microbiology, 2009, 138 (3-4), pp.345. ⟨10.1016/j.vetmic.2009.03.030⟩. ⟨hal-00514604⟩