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Research Support, Non-U.S. Gov't
Identification of tyrosine 71 as a critical residue for the cytotoxic activity of Clostridium perfringens epsilon toxin towards MDCK cells
Zhigang Jiang , Jitao Chang , Fang Wang , Li Yu
J. Microbiol. 2015;53(2):141-146.   Published online January 28, 2015
DOI: https://doi.org/10.1007/s12275-015-4523-8
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AbstractAbstract
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.

Citations

Citations to this article as recorded by  
  • Clostridium perfringens epsilon prototoxin mutant rpETXY30A/Y71A/H106P/Y196A as a vaccine candidate against enterotoxemia
    Jige Du, Tuanjie Wang, Lei Xu, Cong Wang, Ying Liu, Chenfan Pan, Xiaoyun Chen, Zhen Zhu, Yufeng Luo, Chunsheng Yin
    Vaccine.2023; 41(32): 4762.     CrossRef
  • Etx-Y71A as a non-toxic mutant of Clostridium perfringens epsilon toxin induces protective immunity in mice and sheep
    Zhigang Jiang, Jitao Chang, Fang Wang, Yinglin Qi, Yixin Li, Debin Yu, Li Yu
    Vaccine.2020; 38(42): 6553.     CrossRef
  • Crystal structure of a cytocidal protein from lamprey and its mechanism of action in the selective killing of cancer cells
    Yue Pang, Meng Gou, Kai Yang, Jiali Lu, Yinglun Han, Hongming Teng, Changzhi Li, Haina Wang, Caigang Liu, Kejia Zhang, Yongliang Yang, Qingwei Li
    Cell Communication and Signaling.2019;[Epub]     CrossRef
  • The pore structure of Clostridium perfringens epsilon toxin
    Christos G. Savva, Alice R. Clark, Claire E. Naylor, Michel R. Popoff, David S. Moss, Ajit K. Basak, Richard W. Titball, Monika Bokori-Brown
    Nature Communications.2019;[Epub]     CrossRef
  • A Novel Panel of Rabbit Monoclonal Antibodies and Their Diverse Applications Including Inhibition of Clostridium perfringens Epsilon Toxin Oligomerization
    Jennifer R. Linden, Kiel Telesford, Samantha Shetty, Paige Winokour, Sylvia Haigh, Ellen Cahir-McFarland, Giovanna Antognetti, Abhishek Datta, Tao Wang, Werner Meier, Timothy Vartanian
    Antibodies.2018; 7(4): 37.     CrossRef
  • Recombinant Alpha, Beta, and Epsilon Toxins of Clostridium perfringens: Production Strategies and Applications as Veterinary Vaccines
    Marcos Ferreira, Gustavo Moreira, Carlos Cunha, Marcelo Mendonça, Felipe Salvarani, Ângela Moreira, Fabricio Conceição
    Toxins.2016; 8(11): 340.     CrossRef

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