ReviewFrontiers in microbiology2015
Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.
Review in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- The Extracytoplasmic Protein Quality Control System in Pathogenic Campylobacterota: Its Role in Bacterial Virulence and Maintaining Cellular Envelope Proteostasis.International journal of molecular sciences · 2025Review
- Characterisation of the Gastrointestinal Microbiome of Green Sea Turtles (Animals : an open access journal from MDPI · 2025Review
- Survival ofMicroorganisms · 2022Article
- Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases ofInternational journal of molecular sciences · 2021Article
- Genetic Dissection of the Fermentative and Respiratory Contributions Supporting Vibrio cholerae Hypoxic Growth.Journal of bacteriology · 2020Article
- C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning.PloS one · 2020Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- The Multiple Localized Glyceraldehyde-3-Phosphate Dehydrogenase Contributes to the Attenuation of theFrontiers in cellular and infection microbiology · 2017Article
- Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231).Frontiers in microbiology · 2016Article
- Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain.Frontiers in microbiology · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial proteins of the Dsb family-important components of the post-translational protein modification system-catalyze the formation of disulfide bridges, a process that is crucial for protein structure stabilization and activity. Dsb systems play an essential role in the assembly of many virulence factors. Recent rapid advances in global analysis of bacteria have thrown light on the enormous diversity among bacterial Dsb systems. While the Escherichia coli disulfide bond-forming system is quite well understood, the mechanisms of action of Dsb systems in other bacteria, including members of class Epsilonproteobacteria that contain pathogenic and non-pathogenic bacteria colonizing extremely diverse ecological niches, are poorly characterized. Here we present a review of current knowledge on Epsilonproteobacteria Dsb systems. We have focused on the Dsb systems of Campylobacter spp. and Helicobacter spp. because our knowledge about Dsb proteins of Wolinella and Arcobacter spp. is still scarce and comes mainly from bioinformatic studies. Helicobacter pylori is a common human pathogen that colonizes the gastric epithelium of humans with severe consequences. Campylobacter spp. is a leading cause of zoonotic enteric bacterial infections in most developed and developing nations. We focus on various aspects of the diversity of the Dsb systems and their influence on pathogenicity, particularly because Dsb proteins are considered as potential targets for a new class of anti-virulence drugs to treat human infections by Campylobacter or Helicobacter spp.
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