DsbA: a protein-folding catalyst contributing to bacterial virulence

• Published in: Microbes and Infection Vol. 1; no. 14; pp. 1221 - 1228
• Main Authors: Yu, Jun, Kroll, J.Simon
• Format: Book Review Journal Article
• Language: English
• Published: Lausanne Elsevier SAS 01.12.1999; Amsterdam Elsevier; Paris
• Subjects: Animals; Bacterial Proteins - metabolism; Bacterial Proteins - secretion; Bacterial Toxins - metabolism; Bacteriology; Biological and medical sciences; Biological Transport, Active; Dsb protein; DsbA; Fimbriae, Bacterial - physiology; Fundamental and applied biological sciences. Psychology; Gram-Negative Bacteria - cytology; Gram-Negative Bacteria - enzymology; Gram-Negative Bacteria - metabolism; Gram-Negative Bacteria - pathogenicity; HeLa Cells - microbiology; HeLa Cells - ultrastructure; Humans; Microbiology; Microscopy, Electron; Mutation; Oxidation-Reduction; pathogenicity; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Periplasm - enzymology; Plants - microbiology; Protein Disulfide-Isomerases - chemistry; Protein Disulfide-Isomerases - genetics; Protein Disulfide-Isomerases - physiology; Protein Folding; Shigella flexneri; Shigella flexneri - cytology; Shigella flexneri - enzymology; Shigella flexneri - metabolism; Shigella flexneri - pathogenicity; thiol-disulfide oxidoreductase; Virulence; pathogenicity; protein-folding; DsbA; Pathogenicity; Refolding; Virulence; Bacteria; Shigella flexneri; Review; Structure function relationship; Enterobacteriaceae
• ISSN: 1286-4579; 1769-714X
• DOI: 10.1016/S1286-4579(99)00239-7

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.