ArticleThe Journal of biological chemistry2015
C3larvin toxin, an ADP-ribosyltransferase from Paenibacillus larvae.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 48 citations in OpenAlex.
- Unravelling bacterial virulence factors in yeast: From identification to the elucidation of their mechanisms of action.Archives of microbiology · 2024Review
- Pierisin, Cytotoxic and Apoptosis-Inducing DNA ADP-Ribosylating Protein in Cabbage Butterfly.Toxins · 2024Review
- American Foulbrood-Old and Always New Challenge.Veterinary sciences · 2023Review
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- A Structural Approach to Anti-Virulence: A Discovery Pipeline.Microorganisms · 2021Article
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- Role of mono-ADP-ribosylation histone modification (Review).Experimental and therapeutic medicine · 2021Review
- The Buzz about ADP-Ribosylation Toxins fromToxins · 2021Review
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- Review
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- Putative determinants of virulence inVirulence · 2020Article
- Article
- Characterization of C3larvinA, a novel RhoA-targeting ADP-ribosyltransferase toxin produced by the honey bee pathogen, Paenibacillus larvae.Bioscience reports · 2020Article
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- Swarming motility and biofilm formation of Paenibacillus larvae, the etiological agent of American Foulbrood of honey bees (Apis mellifera).Scientific reports · 2018Article
- The Rho ADP-ribosylating C3 exoenzyme binds cells via an Arg-Gly-Asp motif.The Journal of biological chemistry · 2017Article
- Current knowledge and perspectives of Paenibacillus: a review.Microbial cell factories · 2016Review
- C3 exoenzyme impairs cell proliferation and apoptosis by altering the activity of transcription factors.Naunyn-Schmiedeberg's archives of pharmacology · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
C3larvin toxin was identified by a bioinformatic strategy as a putative mono-ADP-ribosyltransferase and a possible virulence factor from Paenibacillus larvae, which is the causative agent of American Foulbrood in honey bees. C3larvin targets RhoA as a substrate for its transferase reaction, and kinetics for both the NAD(+) (Km = 34 ± 12 μm) and RhoA (Km = 17 ± 3 μm) substrates were characterized for this enzyme from the mono-ADP-ribosyltransferase C3 toxin subgroup. C3larvin is toxic to yeast when expressed in the cytoplasm, and catalytic variants of the enzyme lost the ability to kill the yeast host, indicating that the toxin exerts its lethality through its enzyme activity. A small molecule inhibitor of C3larvin enzymatic activity was discovered called M3 (Ki = 11 ± 2 μm), and to our knowledge, is the first inhibitor of transferase activity of the C3 toxin family. C3larvin was crystallized, and its crystal structure (apoenzyme) was solved to 2.3 Å resolution. C3larvin was also shown to have a different mechanism of cell entry from other C3 toxins.
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Registered trials
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