ArticleMolecular microbiology2014
Identification of disulfide bond isomerase substrates reveals bacterial virulence factors.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- An integrative bioinformatics framework for functional annotation and prioritization of hypothetical proteins in Bacillus thuringiensis relevant to biological pest control.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- 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
- Unveiling the versatility of the thioredoxin framework: Insights from the structural examination ofComputational and structural biotechnology journal · 2024Article
- The 27th Annual Midwest Microbial Pathogenesis Conference in the Age of COVID.Journal of bacteriology · 2022Review
- Identification and characterization of two drug-like fragments that bind to the same cryptic binding pocket of Burkholderia pseudomallei DsbA.Acta crystallographica. Section D, Structural biology · 2022Article
- Tick extracellular vesicles enable arthropod feeding and promote distinct outcomes of bacterial infection.Nature communications · 2021Article
- APathogens (Basel, Switzerland) · 2020Article
- Mechanisms Affecting the Acquisition, Persistence and Transmission ofMicroorganisms · 2020Review
- Tn-Seq reveals hidden complexity in the utilization of host-derived glutathione in Francisella tularensis.PLoS pathogens · 2020Article
- Prediction of Burkholderia pseudomallei DsbA substrates identifies potential virulence factors and vaccine targets.PloS one · 2020Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Two DsbA Proteins Are Important forFrontiers in microbiology · 2019Article
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- Dual Role for DsbA in Attacking and Targeted Bacterial Cells during Type VI Secretion System-Mediated Competition.Cell reports · 2018Article
- Article
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- A Nonsense Mutation in Mycobacterium marinum That Is Suppressible by a Novel Mechanism.Infection and immunity · 2017Article
- The Multiple Localized Glyceraldehyde-3-Phosphate Dehydrogenase Contributes to the Attenuation of theFrontiers in cellular and infection microbiology · 2017Article
- Thioredoxin A Is Essential for Motility and Contributes to Host Infection ofFrontiers in cellular and infection microbiology · 2017Article
- The orange spotted cockroach (Proceedings of the West Virginia Academy of Science · 2017Article
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3 authors.
Funding
Abstract
Bacterial pathogens are exposed to toxic molecules inside the host and require efficient systems to form and maintain correct disulfide bonds for protein stability and function. The intracellular pathogen Francisella tularensis encodes a disulfide bond formation protein ortholog, DsbA, which previously was reported to be required for infection of macrophages and mice. However, the molecular mechanisms by which F. tularensis DsbA contributes to virulence are unknown. Here, we demonstrate that F. tularensis DsbA is a bifunctional protein that oxidizes and, more importantly, isomerizes complex disulfide connectivity in substrates. A single amino acid in the conserved cis-proline loop of the DsbA thioredoxin domain was shown to modulate both isomerase activity and F. tularensis virulence. Trapping experiments in F. tularensis identified over 50 F. tularensis DsbA substrates, including outer membrane proteins, virulence factors, and many hypothetical proteins. Six of these hypothetical proteins were randomly selected and deleted, revealing two novel proteins, FTL_1548 and FTL_1709, which are required for F. tularensis virulence. We propose that the extreme virulence of F. tularensis is partially due to the bifunctional nature of DsbA, that many of the newly identified substrates are required for virulence, and that the development of future DsbA inhibitors could have broad anti-bacterial implications.
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