ArticleMolecular microbiology2015
A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 46 citations in OpenAlex.
- Article
- Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding.Protein science : a publication of the Protein Society · 2026Article
- Virulence and mutations analysis based on the whole genome of a BrazilianFrontiers in microbiology · 2025Article
- Article
- Infection by a multidrug-resistant Corynebacterium diphtheriae strain: prediction of virulence factors, CRISPR-Cas system analysis, and structural implications of mutations conferring rifampin resistance.Functional & integrative genomics · 2024Article
- Development of a sensor for disulfide bond formation in diverse bacteria.Journal of bacteriology · 2024Article
- Phenotypic and molecular characterization and complete genome sequence of a Corynebacterium diphtheriae strain isolated from cutaneous infection in an immunized individual.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- A cryptic oxidoreductase safeguards oxidative protein folding inProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Analysis ofPeerJ · 2023Article
- A review on pilus assembly mechanisms in Gram-positive and Gram-negative bacteria.Cell surface (Amsterdam, Netherlands) · 2022Article
- A cell wall-anchored glycoprotein confers resistance to cation stress in Actinomyces oris biofilms.Molecular oral microbiology · 2022Article
- Endospore Appendages: a novel pilus superfamily from the endospores of pathogenic Bacilli.The EMBO journal · 2021Article
- Identification of a Thiol-Disulfide Oxidoreductase (SdbA) Catalyzing Disulfide Bond Formation in the Superantigen SpeA in Streptococcus pyogenes.Journal of bacteriology · 2021Article
- Anchoring surface proteins to the bacterial cell wall by sortase enzymes: how it started and what we know now.Current opinion in microbiology · 2021Review
- Ribonuclease J-Mediated mRNA Turnover Modulates Cell Shape, Metabolism and Virulence inMicroorganisms · 2021Article
- New Paradigms of Pilus Assembly Mechanisms in Gram-Positive Actinobacteria.Trends in microbiology · 2020Review
- Corynebacterium diphtheriae Virulence Analyses Using a Caenorhabditis elegans Model.Current protocols in microbiology · 2020Article
- Genetic Manipulation of Corynebacterium diphtheriae and Other Corynebacterium Species.Current protocols in microbiology · 2020Article
- Proteomics of extracellular vesicles produced by Granulicatella adiacens, which causes infective endocarditis.PloS one · 2020Article
- The distinction of CPR bacteria from other bacteria based on protein family content.Nature communications · 2019Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The Gram-positive pathogen Corynebacterium diphtheriae exports through the Sec apparatus many extracellular proteins that include the key virulence factors diphtheria toxin and the adhesive pili. How these proteins attain their native conformations after translocation as unfolded precursors remains elusive. The fact that the majority of these exported proteins contain multiple cysteine residues and that several membrane-bound oxidoreductases are encoded in the corynebacterial genome suggests the existence of an oxidative protein-folding pathway in this organism. Here we show that the shaft pilin SpaA harbors a disulfide bond in vivo and alanine substitution of these cysteines abrogates SpaA polymerization and leads to the secretion of degraded SpaA peptides. We then identified a thiol-disulfide oxidoreductase (MdbA), whose structure exhibits a conserved thioredoxin-like domain with a CPHC active site. Remarkably, deletion of mdbA results in a severe temperature-sensitive cell division phenotype. This mutant also fails to assemble pilus structures and is greatly defective in toxin production. Consistent with these defects, the ΔmdbA mutant is attenuated in a guinea pig model of diphtheritic toxemia. Given its diverse cellular functions in cell division, pilus assembly and toxin production, we propose that MdbA is a component of the general oxidative folding machine in C. diphtheriae.
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