A host-specific factor is necessary for efficient folding of the autotransporter plasmid-encoded toxin
Abbreviated Journal Title
Autotransporter; Circular dichroism; Plasmid-encoded toxin; Protein; folding; ENTEROAGGREGATIVE ESCHERICHIA-COLI; SHIGELLA-FLEXNERI; PROTEIN; SECRETION; EPITHELIAL-CELLS; COMMON THEMES; BETA-HELIX; PET; PATHWAY; SURFACE; ICSA; Biochemistry & Molecular Biology
Autotransporters are the most common virulence factors secreted from Gram-negative pathogens. Until recently, autotransporter folding and outer membrane translocation were thought to be self-mediated events that did not require accessory factors. Here, we report that two variants of the autotransporter plasmid-encoded toxin are secreted by a lab strain of Escherichia coli. Biophysical analysis and cell-based toxicity assays demonstrated that only one of the two variants was in a folded, active conformation. The misfolded variant was not produced by a pathogenic strain of enteroaggregative E. coli and did not result from protein overproduction in the lab strain of E coli. Our data suggest a host-specific factor is required for efficient folding of plasmid-encoded toxin. (C) 2009 Elsevier Masson SAS. All rights reserved.
"A host-specific factor is necessary for efficient folding of the autotransporter plasmid-encoded toxin" (2010). Faculty Bibliography 2010s. 589.