ArticleInfection and immunity2002
DsbA and DsbC are required for secretion of pertussis toxin by Bordetella pertussis.
Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed.
- Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding.Protein science : a publication of the Protein Society · 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
- Deep longitudinal multi-omics analysis ofFrontiers in microbiology · 2023Article
- Periplasmic Targets for the Development of Effective Antimicrobials against Gram-Negative Bacteria.ACS infectious diseases · 2020Review
- Mutagenesis of DsbAss is Crucial for the Signal Recognition Particle Mechanism inBiomolecules · 2019Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents.Molecules (Basel, Switzerland) · 2016Review
- Helicobacter pylori HP0231 Influences Bacterial Virulence and Is Essential for Gastric Colonization.PloS one · 2016Article
- Monitoring Oxidative Folding of a Single Protein Catalyzed by the Disulfide Oxidoreductase DsbA.The Journal of biological chemistry · 2015Article
- Targeting virulence not viability in the search for future antibacterials.British journal of clinical pharmacology · 2015Review
- Disarming Burkholderia pseudomallei: structural and functional characterization of a disulfide oxidoreductase (DsbA) required for virulence in vivo.Antioxidants & redox signaling · 2014Article
- Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii.The Journal of biological chemistry · 2013Article
- DsbA2 (27 kDa Com1-like protein) of Legionella pneumophila catalyses extracytoplasmic disulphide-bond formation in proteins including the Dot/Icm type IV secretion system.Molecular microbiology · 2011Article
- Application of fragment-based drug discovery to membrane proteins: identification of ligands of the integral membrane enzyme DsbB.Chemistry & biology · 2010Article
- DSB proteins and bacterial pathogenicity.Nature reviews. Microbiology · 2009Review
- Disulfide bond isomerization in prokaryotes.Biochimica et biophysica acta · 2008Review
- Activation of the Cpx envelope stress response down-regulates expression of several locus of enterocyte effacement-encoded genes in enteropathogenic Escherichia coli.Infection and immunity · 2008Article
- The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis.Infection and immunity · 2008Article
- Moraxella osloensis gene expression in the slug host Deroceras reticulatum.BMC microbiology · 2008Article
- Construction and validation of a first-generation Bordetella bronchiseptica long-oligonucleotide microarray by transcriptional profiling the Bvg regulon.BMC genomics · 2007Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The Dsb family of enzymes catalyzes disulfide bond formation in the gram-negative periplasm, which is required for folding and assembly of many secreted proteins. Pertussis toxin is arguably the most complex toxin known: it is assembled from six subunits encoded by five genes (for subunits S1 to S5), with 11 intramolecular disulfide bonds. To examine the role of the Dsb enzymes in assembly and secretion of pertussis toxin, we identified and mutated the Bordetella pertussis dsbA, dsbB, and dsbC homologues. Mutations in dsbA or dsbB resulted in decreased levels of S1 (the A subunit) and S2 (a B-subunit protein), demonstrating that DsbA and DsbB are required for toxin assembly. Mutations in dsbC did not impair assembly of periplasmic toxin but resulted in decreased toxin secretion, suggesting a defect in the formation of the Ptl secretion complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.