ArticleInfection and immunity2001
Characterization of the enzymatic component of the ADP-ribosyltransferase toxin CDTa from Clostridium difficile.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 127 citations in OpenAlex.
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- Prevalence, Antimicrobial Resistance and Toxin-Encoding Genes ofAntibiotics (Basel, Switzerland) · 2023Article
- CDT ofToxins · 2023Article
- Pain killers: the interplay between nonsteroidal anti-inflammatory drugs and Clostridioides difficile infection.Current opinion in microbiology · 2022Review
- Requirement of Peptidyl-Prolyl Cis/Trans isomerases and chaperones for cellular uptake of bacterial AB-type toxins.Frontiers in cellular and infection microbiology · 2022Review
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- Molecular Detection of ToxigenicVeterinary sciences · 2021Article
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- The Importance of Therapeutically Targeting the Binary Toxin fromInternational journal of molecular sciences · 2021Review
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- The Binary Toxin ofFrontiers in microbiology · 2021Article
- Structure of the cell-binding component of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Human α-Defensin-5 Efficiently NeutralizesFrontiers in pharmacology · 2020Article
- An NADMolecular cell · 2019Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Certain strains of Clostridium difficile produce the ADP-ribosyltransferase CDT, which is a binary actin ADP-ribosylating toxin. The toxin consists of the binding component CDTb, which mediates receptor binding and cellular uptake, and the enzyme component CDTa. Here we studied the enzyme component (CDTa) of the toxin using the binding component of Clostridium perfringens iota toxin (Ib), which is interchangeable with CDTb as a transport component. Ib was used because CDTb was not expressed as a recombinant protein in Escherichia coli. Similar to iota toxin, CDTa ADP-ribosylates nonmuscle and skeletal muscle actin. The N-terminal part of CDTa (CDTa1-240) competes with full-length CDTa for binding to the iota toxin binding component. The C-terminal part (CDTa244-263) harbors the enzyme activity but was much less active than the full-length CDTa. Changes of Glu428 and Glu430 to glutamine, Ser388 to alanine, and Arg345 to lysine blocked ADP-ribosyltransferase activity. Comparison of CDTa with C. perfringens iota toxin and Clostridium botulinum C2 toxin revealed full enzyme activity of the fragment Ia208-413 but loss of activity of several N-terminally deleted C2I proteins including C2I103-431, C2I190-431, and C2I30-431. The data indicate that CDTa belongs to the iota toxin subfamily of binary actin ADP-ribosylating toxins with respect to interaction with the binding component and substrate specificity. It shares typical conserved amino acid residues with iota toxin and C2 toxin that are suggested to be involved in NAD-binding and/or catalytic activity. The enzyme components of CDT, iota toxin, and C2 toxin differ with respect to the minimal structural requirement for full enzyme activity.
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