ArticlePloS one2013
A segment of 97 amino acids within the translocation domain of Clostridium difficile toxin B is essential for toxicity.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 22 citations in OpenAlex.
- The impact of TcdB conformational dynamics on vaccination against Clostridioides difficile.PLoS pathogens · 2026Article
- Article
- Mouse monoclonal antibodies againstInfection and immunity · 2025Article
- High-resolution structure of native toxin A from Clostridioides difficile.EMBO reports · 2022Article
- Structural basis for CSPG4 as a receptor for TcdB and a therapeutic target in Clostridioides difficile infection.Nature communications · 2021Article
- Deletion of a 19-Amino-Acid Region in Clostridioides difficile TcdB2 Results in Spontaneous Autoprocessing and Reduced Cell Binding and Provides a Nontoxic Immunogen for Vaccination.Infection and immunity · 2019Article
- Structure of the full-length Clostridium difficile toxin B.Nature structural & molecular biology · 2019Article
- Cell-penetrating peptides derived fromThe Journal of biological chemistry · 2018Article
- A neutralizing antibody that blocks delivery of the enzymatic cargo ofThe Journal of biological chemistry · 2018Article
- A Novel Bacteriophage Lysin-Human Defensin Fusion Protein Is Effective in Treatment ofFrontiers in microbiology · 2018Article
- Novel Chimeric Protein Vaccines AgainstFrontiers in immunology · 2018Article
- The role of purified Clostridium difficile glucosylating toxins in disease pathogenesis utilizing a murine cecum injection model.Anaerobe · 2017Article
- Article
- Identification of an Essential Region for Translocation of Clostridium difficile Toxin B.Toxins · 2016Article
- Defective mutations within the translocation domain of Clostridium difficile toxin B impair disease pathogenesis.Pathogens and disease · 2016Article
- Masking autoprocessing of Clostridium difficile toxin A by the C-terminus combined repetitive oligo peptides.Biochemical and biophysical research communications · 2015Article
- Exposure of neutralizing epitopes in the carboxyl-terminal domain of TcdB is altered by a proximal hypervariable region.The Journal of biological chemistry · 2015Article
- Critical roles of Clostridium difficile toxin B enzymatic activities in pathogenesis.Infection and immunity · 2015Article
- Translocation domain mutations affecting cellular toxicity identify the Clostridium difficile toxin B pore.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Immune-based treatment and prevention of Clostridium difficile infection.Human vaccines & immunotherapeutics · 2014Review
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Clostridium difficile toxin B (TcdB) intoxicates target cells by glucosylating Rho GTPases. TcdB (269 kDa) consists of at least 4 functional domains including a glucosyltransferase domain (GTD), a cysteine protease domain (CPD), a translocation domain (TD), and a receptor binding domain (RBD). The function and molecular mode of action of the TD, which is the largest segment of TcdB and comprises nearly 50% of the protein, remain largely unknown. Here we show that a 97-amino-acid segment (AA1756 - 1852, designated as ?97 or D97), located in the C-terminus of the TD and adjacent to the RBD, is essential for the cellular activity of TcdB. Deletion of this segment in TcdB (designated as TxB-D97), did not adversely alter toxin enzymatic activities or its cellular binding and uptake capacity. TxB-D97 bound to and entered cells in a manner similar to TcdB holotoxin. Both wild type and mutant toxins released their GTDs similarly in the presence of inositol hexakisphosphate (InsP6), and showed a similar glucosyltransferase activity in a cell-free glucosylating assay. Despite these similarities, the cytotoxic activity of TxB-D97 was reduced by more than 5 logs compared to wild type toxin, supported by the inability of TxB-D97 to glucosylate Rac1 of target cells. Moreover, the mutant toxin failed to elicit tumor necrosis factor alpha (TNF-α) in macrophages, a process dependent on the glucosyltransferase activity of the toxin. Cellular fractionation of toxin-exposed cells revealed that TxB-D97 was unable to efficiently release the GTD into cytosol. Thereby, we conclude the 97-amino-acid region of the TD C-terminus of TcdB adjacent to the RBD, is essential for the toxicity of TcdB.
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