Open AccessThe role of Dsb proteins of Gram‐negative bacteria in the process of pathogenesis
Author(s) -
Łasica Anna M.,
JagusztynKrynicka Elżbieta K.
Publication year - 2007
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1111/j.1574-6976.2007.00081.x
Subject(s) - periplasmic space , virulence , bacteria , biology , cysteine , protein folding , gram negative bacteria , microbiology and biotechnology , protein structure , biochemistry , gene , escherichia coli , genetics , enzyme
Tertiary and quaternary structures of extracytoplasmic proteins containing more than one cysteine residue often require introduction of disulfide bonds. This process takes place in an oxidative environment, such as the periplasm of Gram‐negative bacteria, and is catalyzed by Dsb (disulfide bond formation) proteins. Mutations in dsb genes influence the conformation and stability of many extracytoplasmic proteins. Thus, many pathogens become partially or fully attenuated due to improper folding of proteins that act as virulence factors. This review summarizes the current knowledge on Dsb proteins and their effect on the pathogenicity of Gram‐negative bacteria. The potential application of Dsb proteins in biotechnology is also discussed.