ArticleProtein science : a publication of the Protein Society2023
Structural and functional characterization of the cytotoxic protein ledodin, an atypical ribosome-inactivating protein from shiitake mushroom (Lentinula edodes).
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 15 citations in OpenAlex.
- Purification, Amino Acid Sequence, and Structural Features of a Novel Expansin-like A from the Seeds of Canihua (International journal of molecular sciences · 2026Article
- Modern Pro-Health Applications of Medicinal Mushrooms: Insights into theMolecules (Basel, Switzerland) · 2025Review
- Review
- Edodin: A New Type of Toxin from Shiitake Mushroom (Toxins · 2024Article
- Medicinal Mushrooms as Multicomponent Mixtures-Demonstrated with the Example ofJournal of fungi (Basel, Switzerland) · 2024Review
- A Comprehensive Review of the Diversity of Fungal Secondary Metabolites and Their Emerging Applications in Healthcare and Environment.Mycobiology · 2024Review
- The Biological Action and Structural Characterization of Eryngitin 3 and 4, Ribotoxin-like Proteins fromInternational journal of molecular sciences · 2023Article
- Structural and functional characterization of the cytotoxic protein ledodin, an atypical ribosome-inactivating protein from shiitake mushroom (Lentinula edodes).Protein science : a publication of the Protein Society · 2023Article
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8 authors at 3 institutions in 3 countries.
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Abstract
We have purified ledodin, a cytotoxic 22-kDa protein from shiitake mushroom (Lentinula edodes) consisting of a 197 amino acid chain. Ledodin possessed N-glycosylase activity on the sarcin-ricin loop of mammalian 28S rRNA and inhibited protein synthesis. However, it was not active against insect, fungal, and bacterial ribosomes. In vitro and in silico studies suggested that ledodin exhibits a catalytic mechanism like that of DNA glycosylases and plant ribosome-inactivating proteins. Moreover, the sequence and structure of ledodin was not related to any protein of known function, although ledodin-homologous sequences were found in the genome of several species of fungi, some edible, belonging to different orders of the class Agaricomycetes. Therefore, ledodin could be the first of a new family of enzymes widely distributed among this class of basidiomycetes. The interest of these proteins lies both, in the fact that they can be a toxic agent of some edible mushrooms and in their application in medicine and biotechnology.
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