DsbA: a protein-folding catalyst contributing to bacterial virulence

Microbes Infect. 1999 Dec;1(14):1221-8. doi: 10.1016/s1286-4579(99)00239-7.

Abstract

DsbA, a periplasmic thiol:disulphide oxidoreductase, catalyses the folding of various factors, among which are virulence determinants or the components of type III secretory machinery. It is also necessary for intracellular survival and cell-to-cell spread of the intracellular pathogen Shigella flexneri.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / metabolism
  • Bacterial Toxins / metabolism
  • Biological Transport, Active
  • Fimbriae, Bacterial / physiology
  • Gram-Negative Bacteria / cytology
  • Gram-Negative Bacteria / enzymology
  • Gram-Negative Bacteria / metabolism
  • Gram-Negative Bacteria / pathogenicity*
  • HeLa Cells / microbiology
  • HeLa Cells / ultrastructure
  • Humans
  • Microscopy, Electron
  • Mutation
  • Oxidation-Reduction
  • Periplasm / enzymology
  • Plants / microbiology
  • Protein Disulfide-Isomerases / chemistry
  • Protein Disulfide-Isomerases / genetics
  • Protein Disulfide-Isomerases / physiology*
  • Protein Folding
  • Shigella flexneri / cytology
  • Shigella flexneri / enzymology
  • Shigella flexneri / metabolism
  • Shigella flexneri / pathogenicity*
  • Virulence

Substances

  • Bacterial Proteins
  • Bacterial Toxins
  • Protein Disulfide-Isomerases