S1 pocket of a bacterially derived subtilisin-like protease underpins effective tissue destruction.

ABSTRACT: The ovine footrot pathogen, Dichelobacter nodosus, secretes three subtilisin-like proteases that play an important role in the pathogenesis of footrot through their ability to mediate tissue destruction. Virulent and benign strains of D. nodosus secrete the basic proteases BprV and BprB, respectively, with the catalytic domain of these enzymes having 96% sequence identity. At present, it is not known how sequence variation between these two putative virulence factors influences their respective biological activity. We have determined the high resolution crystal structures of BprV and BprB. These data reveal that that the S1 pocket of BprV is more hydrophobic but smaller than that of BprB. We show that BprV is more effective than BprB in degrading extracellular matrix components of the host

SUBMITTER: Wong W 

PROVIDER: S-EPMC3234984 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature