ArticleThe Journal of biological chemistry2012
Certhrax toxin, an anthrax-related ADP-ribosyltransferase from Bacillus cereus.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Discovery of Novel c-di-GMP-Related Genes inPathogens (Basel, Switzerland) · 2026Article
- From cereus to anthrax and back again: Assessment of the temperature-dependent phenotypic switching in the "cross-over" strainFrontiers in microbiology · 2023Article
- Structures of distant diphtheria toxin homologs reveal functional determinants of an evolutionarily conserved toxin scaffold.Communications biology · 2022Article
- A Structural Approach to Anti-Virulence: A Discovery Pipeline.Microorganisms · 2021Article
- Review
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- Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021Review
- ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021Review
- Review
- Article
- The C. difficile toxin B membrane translocation machinery is an evolutionarily conserved protein delivery apparatus.Nature communications · 2020Article
- You Can'tFrontiers in microbiology · 2020Review
- Article
- TheMicrobiology spectrum · 2019Review
- Certhrax Is an Antivirulence Factor for the Anthrax-Like Organism Bacillus cereus Strain G9241.Infection and immunity · 2018Article
- Expression and contribution to virulence of each polysaccharide capsule of Bacillus cereus strain G9241.PloS one · 2018Article
- Assembly and Function of the Bacillus anthracis S-Layer.Annual review of microbiology · 2017Review
- The roles of AtxA orthologs in virulence of anthrax-like Bacillus cereus G9241.Molecular microbiology · 2016Article
- Scabin, a Novel DNA-acting ADP-ribosyltransferase from Streptomyces scabies.The Journal of biological chemistry · 2016Article
- C3larvin toxin, an ADP-ribosyltransferase from Paenibacillus larvae.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
We identified Certhrax, the first anthrax-like mART toxin from the pathogenic G9241 strain of Bacillus cereus. Certhrax shares 31% sequence identity with anthrax lethal factor from Bacillus anthracis; however, we have shown that the toxicity of Certhrax resides in the mART domain, whereas anthrax uses a metalloprotease mechanism. Like anthrax lethal factor, Certhrax was found to require protective antigen for host cell entry. This two-domain enzyme was shown to be 60-fold more toxic to mammalian cells than anthrax lethal factor. Certhrax localizes to distinct regions within mouse RAW264.7 cells by 10 min postinfection and is extranuclear in its cellular location. Substitution of catalytic residues shows that the mART function is responsible for the toxicity, and it binds NAD(+) with high affinity (K(D) = 52.3 ± 12.2 μM). We report the 2.2 Å Certhrax structure, highlighting its structural similarities and differences with anthrax lethal factor. We also determined the crystal structures of two good inhibitors (P6 (K(D) = 1.7 ± 0.2 μM, K(i) = 1.8 ± 0.4 μM) and PJ34 (K(D) = 5.8 ± 2.6 μM, K(i) = 9.6 ± 0.3 μM)) in complex with Certhrax. As with other toxins in this family, the phosphate-nicotinamide loop moves toward the NAD(+) binding site with bound inhibitor. These results indicate that Certhrax may be important in the pathogenesis of B. cereus.
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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.