Article
Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.
The Journal of biological chemistry - 21 Apr 2017
Landeta Cristina, Meehan Brian M, McPartland Laura, Ingendahl Linda, Hatahet Feras, Tran Ngoc Q, Boyd Dana, Beckwith Jon
Abstract excerpt
Disulfide bonds contribute to protein stability, activity, and folding in a variety of proteins, including many involved in bacterial virulence such as toxins, adhesins, flagella, and pili, among others. Therefore, inhibitors of disulfide bond formation enzymes could have profound effects on pathogen virulence. In the Escherichia coli disulfide bond formation pathway, the periplasmic protein DsbA introduces...
Topics
- Anti-Bacterial Agents
- Bacterial Outer Membrane Proteins
- Bacterial Proteins
- Disulfides
- Escherichia coli
- Escherichia coli Proteins
- Gene Library
- Kinetics
- Lipopolysaccharides
- Membrane Proteins
- Mutagenesis
- Mutation
- Polymerase Chain Reaction