The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis.
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.
Łasica
Anna M
AM
Department of Bacterial Genetics, Institute of Microbiology, Biology Faculty, University of Warsaw, Miecznikowa 1, 02-096 Warsaw, Poland. kjkryn@biol.uw.edu.pl
Jagusztyn-Krynicka
Elzbieta K
EK
D001426:Bacterial Proteins / Q000378:metabolism*; D006090:Gram-Negative Bacteria / Q000737:chemistry* / Q000472:pathogenicity*; D008565:Membrane Proteins / Q000378:metabolism*; D017510:Protein Folding; D037521:Virulence Factors / Q000378:metabolism
D001426:Bacterial Proteins; D008565:Membrane Proteins; D037521:Virulence Factors