ArticlePLoS computational biology2010
Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases.
Article in PLoS computational biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 58 citations in OpenAlex.
- A deep learning method to predict bacterial ADP-ribosyltransferase toxins.Bioinformatics (Oxford, England) · 2024Article
- The DarT/DarG Toxin-Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies.Pathogens (Basel, Switzerland) · 2023Article
- From cereus to anthrax and back again: Assessment of the temperature-dependent phenotypic switching in the "cross-over" strainFrontiers in microbiology · 2023Article
- Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop.Nucleic acids research · 2022Article
- 14-3-3 Activated Bacterial Exotoxins AexT and ExoT Share Actin and the SH2 Domains of CRK Proteins as Targets for ADP-Ribosylation.Pathogens (Basel, Switzerland) · 2022Article
- ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological Perspectives.Biomolecules · 2022Review
- A Structural Approach to Anti-Virulence: A Discovery Pipeline.Microorganisms · 2021Article
- TheGenes · 2021Review
- Community-Acquired Respiratory Distress Syndrome Toxin: Unique Exotoxin forFrontiers in microbiology · 2021Review
- Review
- Article
- You Can'tFrontiers in microbiology · 2020Review
- Crystal Structure-Based Exploration of Arginine-Containing Peptide Binding in the ADP-Ribosyltransferase Domain of the Type III Effector XopAI Protein.International journal of molecular sciences · 2019Article
- Targeting ADP-ribosylation as an antimicrobial strategy.Biochemical pharmacology · 2019Review
- Article
- MAV_4644 Interaction with the Host Cathepsin Z ProtectsMicroorganisms · 2019Article
- The tuberculosis necrotizing toxin is an NADThe Journal of biological chemistry · 2019Article
- 14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface.Nature communications · 2018Article
- Certhrax Is an Antivirulence Factor for the Anthrax-Like Organism Bacillus cereus Strain G9241.Infection and immunity · 2018Article
- Protein Structure Facilitates High-Resolution Immunological Mapping.Clinical and vaccine immunology : CVI · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chelt, a cholera-like toxin from Vibrio cholerae, and Certhrax, an anthrax-like toxin from Bacillus cereus, are among six new bacterial protein toxins we identified and characterized using in silico and cell-based techniques. We also uncovered medically relevant toxins from Mycobacterium avium and Enterococcus faecalis. We found agriculturally relevant toxins in Photorhabdus luminescens and Vibrio splendidus. These toxins belong to the ADP-ribosyltransferase family that has conserved structure despite low sequence identity. Therefore, our search for new toxins combined fold recognition with rules for filtering sequences--including a primary sequence pattern--to reduce reliance on sequence identity and identify toxins using structure. We used computers to build models and analyzed each new toxin to understand features including: structure, secretion, cell entry, activation, NAD+ substrate binding, intracellular target binding and the reaction mechanism. We confirmed activity using a yeast growth test. In this era where an expanding protein structure library complements abundant protein sequence data--and we need high-throughput validation--our approach provides insight into the newest toxin ADP-ribosyltransferases.
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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.