國家衛生研究院 NHRI:Item 3990099045/1150
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    题名: Mutations at KFRDI and VGK domains of enterovirus 71 3C protease affect its RNA binding and proteolytic activities
    作者: Shih, SR;Chiang, CY;Chen, TC;Wu, CN;Hsu, JTA;Lee, JC;Hwang, MJ;Li, ML;Chen, GW;Hoc, MS
    贡献者: Division of Biotechnology and Pharmaceutical Research
    摘要: The 3C protease (3C(pro)) of enterovirus 71 (EV71) is a good molecular target for drug discovery. Notably, this protease was found to possess RNA-binding activity. The regions responsible for RNA binding were classified as 'KFRDI' (positions 82-86) and 'VGK' (positions 154-156) in 3C(pro) by mutagenesis study. Although the RNA-binding regions are structurally distinct from the catalytic site of EV71 3C(pro), mutations in the RNA-binding regions influenced 3C(pro) proteolytic activity. In contrast, mutations at the catalytic site had almost no influence on RNA binding ability. We identified certain mutations within 3C(pro) which abrogated both the RNA-binding activity of the expressed, recombinant, protease and the ability to rescue virus from an infectious full-length clone of EV71 (pEV71). Interestingly, mutation at position 84 from Arg(R) to Lys(K) was found to retain good RNA binding and proteolytic activity for the recombinant 3C(pro); however, no virus could be rescued when pEV71 with the R84K mutation was introduced into the infectious copy. Together, these results may provide useful information for using 3C(pro) as the molecular target to develop anti-EV71 agents.
    关键词: Medicine, Research & Experimental
    日期: 2004
    關聯: Journal of Biomedical Science. 2004;11(2):239-248.
    Link to: http://dx.doi.org/10.1007/BF02256567
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=1021-7770&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000188957300012
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=10744222072
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