ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 81 citations in OpenAlex.
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- Advances in adhesion-related pathogenesis inFrontiers in microbiology · 2025Review
- Uncovering the potential virulence factors of emerging pathogens using AI/ML-based tools: a case study inFrontiers in cellular and infection microbiology · 2025Article
- Laboratory diagnosis and treatment ofAnnals of medicine · 2024Review
- Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin.Nature communications · 2024Article
- Association of serum interleukin-17 level andTranslational pediatrics · 2024Article
- Structure-Based Virtual Screening, ADMET Properties Prediction and Molecular Dynamics Studies Reveal Potential Inhibitors ofLife (Basel, Switzerland) · 2024Article
- Risk association model for atelectasis complication inFrontiers in pediatrics · 2024Article
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Mycoplasma pneumoniae (Mp) infections cause tracheobronchitis and "walking" pneumonia, and are linked to asthma and other reactive airway diseases. As part of the infectious process, the bacterium expresses a 591-aa virulence factor with both mono-ADP ribosyltransferase (mART) and vacuolating activities known as Community-Acquired Respiratory Distress Syndrome Toxin (CARDS TX). CARDS TX binds to human surfactant protein A and annexin A2 on airway epithelial cells and is internalized, leading to a range of pathogenetic events. Here we present the structure of CARDS TX, a triangular molecule in which N-terminal mART and C-terminal tandem β-trefoil domains associate to form an overall architecture distinct from other well-recognized ADP-ribosylating bacterial toxins. We demonstrate that CARDS TX binds phosphatidylcholine and sphingomyelin specifically over other membrane lipids, and that cell surface binding and internalization activities are housed within the C-terminal β-trefoil domain. The results enhance our understanding of Mp pathogenicity and suggest a novel avenue for the development of therapies to treat Mp-associated asthma and other acute and chronic airway diseases.
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