Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4359254 | Research in Microbiology | 2010 | 6 Pages |
Abstract
The structure of DspF, a type III secretion system (T3SS) chaperone required for virulence of the fruit tree pathogen Erwinia amylovora, was modeled based on predicted structural homology to characterized T3SS chaperones. This model guided the selection of 11 amino acid residues that were individually mutated to alanine via site-directed mutagenesis. Each mutant was assessed for its effect on virulence complementation, dimerization and interaction with the N-terminal chaperone-binding site of DspE. Four amino acid residues were identified that did not complement the virulence defect of a dspF knockout mutant, and three of these residues were required for interaction with the N-terminus of DspE. This study supports the significance of the predicted β-sheet helix-binding groove in DspF chaperone function.
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Authors
Lindsay R. Triplett, William J. Wedemeyer, George W. Sundin,