ArticleAntioxidants & redox signaling2014
Disarming Burkholderia pseudomallei: structural and functional characterization of a disulfide oxidoreductase (DsbA) required for virulence in vivo.
Article in Antioxidants & redox signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 57 citations in OpenAlex.
- 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
- Identification of an Allene Warhead That Selectively Targets a Histidine Residue in theACS medicinal chemistry letters · 2025Article
- Fluoromethylketone-Fragment Conjugates Designed as Covalent Modifiers of EcDsbA are Atypical Substrates.ChemMedChem · 2024Article
- The Balance between Protealysin and Its Substrate, the Outer Membrane Protein OmpX, RegulatesInternational journal of molecular sciences · 2024Review
- A Buried Water Network Modulates the Activity of theAntioxidants (Basel, Switzerland) · 2023Article
- 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
- Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases ofInternational journal of molecular sciences · 2021Article
- Anti-Virulence Therapeutic Approaches forAntibiotics (Basel, Switzerland) · 2021Review
- Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates.Computational and structural biotechnology journal · 2021Review
- NMR fragment screening reveals a novel small molecule binding site near the catalytic surface of the disulfide-dithiol oxidoreductase enzyme DsbA from Burkholderia pseudomallei.Journal of biomolecular NMR · 2020Article
- Periplasmic Targets for the Development of Effective Antimicrobials against Gram-Negative Bacteria.ACS infectious diseases · 2020Review
- Prediction of Burkholderia pseudomallei DsbA substrates identifies potential virulence factors and vaccine targets.PloS one · 2020Article
- The Fragment-Based Development of a Benzofuran Hit as a New Class ofMolecules (Basel, Switzerland) · 2019Article
- Insights into the Periplasmic Proteins ofInternational journal of molecular sciences · 2019Article
- The Edwardsiella piscicida thioredoxin-like protein inhibits ASK1-MAPKs signaling cascades to promote pathogenesis during infection.PLoS pathogens · 2019Article
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- Inhibition of Diverse DsbA Enzymes in Multi-DsbA Encoding Pathogens.Antioxidants & redox signaling · 2018Article
- Virulence of the Melioidosis Pathogen Burkholderia pseudomallei Requires the Oxidoreductase Membrane Protein DsbB.Infection and immunity · 2018Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimsThe intracellular pathogen Burkholderia pseudomallei causes the disease melioidosis, a major source of morbidity and mortality in southeast Asia and northern Australia. The need to develop novel antimicrobials is compounded by the absence of a licensed vaccine and the bacterium's resistance to multiple antibiotics. In a number of clinically relevant Gram-negative pathogens, DsbA is the primary disulfide oxidoreductase responsible for catalyzing the formation of disulfide bonds in secreted and membrane-associated proteins. In this study, a putative B. pseudomallei dsbA gene was evaluated functionally and structurally and its contribution to infection assessed.
resultsBiochemical studies confirmed the dsbA gene encodes a protein disulfide oxidoreductase. A dsbA deletion strain of B. pseudomallei was attenuated in both macrophages and a BALB/c mouse model of infection and displayed pleiotropic phenotypes that included defects in both secretion and motility. The 1.9 Å resolution crystal structure of BpsDsbA revealed differences from the classic member of this family Escherichia coli DsbA, in particular within the region surrounding the active site disulfide where EcDsbA engages with its partner protein E. coli DsbB, indicating that the interaction of BpsDsbA with its proposed partner BpsDsbB may be distinct from that of EcDsbA-EcDsbB. INNOVATION: This study has characterized BpsDsbA biochemically and structurally and determined that it is required for virulence of B. pseudomallei.
conclusionThese data establish a critical role for BpsDsbA in B. pseudomallei infection, which in combination with our structural characterization of BpsDsbA will facilitate the future development of rationally designed inhibitors against this drug-resistant organism.
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