ArticleJournal of microbiology (Seoul, Korea)2015
Identification of tyrosine 71 as a critical residue for the cytotoxic activity of Clostridium perfringens epsilon toxin towards MDCK cells.
Article in Journal of microbiology (Seoul, Korea), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- The pore structure of Clostridium perfringens epsilon toxin.Nature communications · 2019Article
- Crystal structure of a cytocidal protein from lamprey and its mechanism of action in the selective killing of cancer cells.Cell communication and signaling : CCS · 2019Article
- A Novel Panel of Rabbit Monoclonal Antibodies and Their Diverse Applications Including Inhibition ofAntibodies (Basel, Switzerland) · 2018Article
- Review
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
Clostridium perfringens epsilon toxin (Etx) is an extremely potent toxin, causing fatal enterotoxaemia in many animals. Several amino acids in domains I and II have been proposed to be critical for Etx to interact with MDCK cells. However, the critical amino acids in domain III remain undefined. Therefore, we assessed the effects of aromatic amino acids in domain III on Etx activity in this study. All of the results indicated that Y71 was critical for the cytotoxic activity of Etx towards MDCK cells, and this activity was dependent on the existence of an aromatic ring residue in position 71. Additionally, mutations in Y71 did not affect the binding of Etx to MDCK cells, indicating that Y71 is not a receptor binding site for Etx. In summary, we identified an amino acid in domain III that is important for the cytotoxic activity of Etx, thereby providing information on the structure-function relationship of Etx.
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