ArticleMolecular microbiology2005
Characterization of point mutations in the cdtA gene of the cytolethal distending toxin of Actinobacillus actinomycetemcomitans.
Article in Molecular microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- TM9SF4 acts as a receptor mediatingFrontiers in cellular and infection microbiology · 2026Article
- Revisiting bacterial cytolethal distending toxin structure and function.Frontiers in cellular and infection microbiology · 2023Article
- Delivery, structure, and function of bacterial genotoxins.Virulence · 2022Review
- Cytolethal distending toxin: from genotoxin to a potential biomarker and anti-tumor target.World journal of microbiology & biotechnology · 2021Review
- Novel virulence, antibiotic resistance and toxin gene-specific PCR-based assays for rapid pathogenicity assessment of Arcobacter faecis and Arcobacter lanthieri.BMC microbiology · 2019Article
- Review
- Distinct Roles for CdtA and CdtC during Intoxication by Cytolethal Distending Toxins.PloS one · 2015Article
- Review
- Cytolethal distending toxins require components of the ER-associated degradation pathway for host cell entry.PLoS pathogens · 2014Article
- Article
- Cell junction remodeling in gingival tissue exposed to a microbial toxin.Journal of dental research · 2013Article
- Cellular interactions of the cytolethal distending toxins from Escherichia coli and Haemophilus ducreyi.The Journal of biological chemistry · 2013Article
- A new functional site W115 in CdtA is critical for Aggregatibacter actinomycetemcomitans cytolethal distending toxin.PloS one · 2013Article
- Characterization of Aggregatibacter actinomycetemcomitans strains in periodontitis patients in Germany.Clinical oral investigations · 2012Article
- Localization of Aggregatibacter actinomycetemcomitans cytolethal distending toxin subunits during intoxication of live cells.Infection and immunity · 2012Article
- Bacterial toxin modulation of the eukaryotic cell cycle: are all cytolethal distending toxins created equally?Frontiers in cellular and infection microbiology · 2012Review
- Cholesterol depletion reduces entry of Campylobacter jejuni cytolethal distending toxin and attenuates intoxication of host cells.Infection and immunity · 2011Article
- Cytolethal distending toxin damages the oral epithelium of gingival explants.Journal of dental research · 2011Article
- Cytolethal distending toxin: a conserved bacterial genotoxin that blocks cell cycle progression, leading to apoptosis of a broad range of mammalian cell lineages.Microbiology (Reading, England) · 2011Review
- Targeted inhibition of CD133+ cells in oral cancer cell lines.Journal of dental research · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Cdt is a family of gram-negative bacterial toxins that typically arrest eukaryotic cells in the G0/G1 or G2/M phase of the cell cycle. The toxin is a heterotrimer composed of the cdtA, cdtB and cdtC gene products. Although it has been shown that the CdtA protein subunit binds to cells in culture and in an enzyme-linked immunosorbent assay (CELISA) the precise mechanisms by which CdtA interacts with CdtB and CdtC has not yet been clarified. In this study we employed a random mutagenesis strategy to construct a library of point mutations in cdtA to assess the contribution of individual amino acids to binding activity and to the ability of the subunit to form biologically active holotoxin. Single unique amino acid substitutions in seven CdtA mutants resulted in reduced binding of the purified recombinant protein to Chinese hamster ovary cells and loss of binding to the fucose-containing glycoprotein, thyroglobulin. These mutations clustered at the 5'- and 3'-ends of the cdtA gene resulting in amino acid substitutions that resided outside of the aromatic patch region and a conserved region in CdtA homologues. Three of the amino acid substitutions, at positions S165N (mutA81), T41A (mutA121) and C178W (mutA221) resulted in gene products that formed holotoxin complexes that exhibited a 60% reduction (mutA81) or loss (mutA121, mutA221) of proliferation inhibition. A similar pattern was observed when these mutant holotoxins were tested for their ability to induce cell cycle arrest and to convert supercoiled DNA to relaxed and linear forms in vitro. The mutations in mutA81 and mutA221 disrupted holotoxin formation. The positions of the amino acid substitutions were mapped in the Haemophilus ducreyi Cdt crystal structure providing some insight into structure and function.
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