ArticleInfection and immunity2008
Role of aromatic amino acids in receptor binding activity and subunit assembly of the cytolethal distending toxin of Aggregatibacter actinomycetemcomitans.
Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
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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
20 citing papers in PubMed, 30 citations in OpenAlex.
- Bacterial Toxin Exploits Host Membrane Phospholipid as a Receptor for Binding, Entry, and Cytopathogenicity.Molecular microbiology · 2026Article
- TM9SF4 acts as a receptor mediatingFrontiers in cellular and infection microbiology · 2026Article
- Review
- Upregulation of occludin by cytolethal distending toxin facilitatesInfection and immunity · 2023Article
- Article
- GeneFrontiers in microbiology · 2022Article
- Herpesvirus-bacteria synergistic interaction in periodontitis.Periodontology 2000 · 2020Review
- PCP-B class pollen coat proteins are key regulators of the hydration checkpoint in Arabidopsis thaliana pollen-stigma interactions.The New phytologist · 2017Article
- A Journey of Cytolethal Distending Toxins through Cell Membranes.Frontiers in cellular and infection microbiology · 2016Review
- VP22 core domain from Herpes simplex virus 1 reveals a surprising structural conservation in both the Alpha- and Gammaherpesvirinae subfamilies.The Journal of general virology · 2015Article
- 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
- 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
- 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
- Cytolethal distending toxin damages the oral epithelium of gingival explants.Journal of dental research · 2011Article
- Functional and structural characterization of chimeras of a bacterial genotoxin and human type I DNAse.FEMS microbiology letters · 2009Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The periodontal pathogen Aggregatibacter actinomycetemcomitans produces a cytolethal distending toxin (Cdt) that inhibits the proliferation of oral epithelial cells. Structural models suggest that the CdtA and CdtC subunits of the Cdt heterotrimer form two putative lectin domains with a central groove. A region of CdtA rich in heterocyclic amino acids (aromatic patch) appears to play an important role in receptor recognition. In this study site-specific mutagenesis was used to assess the contributions of aromatic amino acids (tyrosine and phenylalanine) to receptor binding and CdtA-CdtC assembly. Predominant surface-exposed aromatic residues that are adjacent to the aromatic patch region in CdtA or are near the groove located at the junction of CdtA and CdtC were studied. Separately replacing residues Y105, Y140, Y188, and Y189 with alanine in CdtA resulted in differential effects on binding related to residue position within the aromatic region. The data indicate that an extensive receptor binding domain extends from the groove across the entire face of CdtA that is oriented 180 degrees from the CdtB subunit. Replacement of residue Y105 in CdtA and residues Y61 and F141 in CdtC, which are located in or at the periphery of the groove, inhibited toxin assembly. Taken together, these results, along with the lack of an aromatic amino acid-rich region in CdtC similar to that in CdtA, suggest that binding of the heterotoxin to its cell surface receptor is mediated predominantly by the CdtA subunit. These findings are important for developing strategies designed to block the activity of this prominent virulence factor.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.