國家衛生研究院 NHRI:Item 3990099045/1150

NHRI > Institute of Biotechnology and Pharmaceutical Research > John Tsu-An Hsu > Periodical Articles > Item 3990099045/1150

Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/1150

Title:	Mutations at KFRDI and VGK domains of enterovirus 71 3C protease affect its RNA binding and proteolytic activities
Authors:	Shih, SR;Chiang, CY;Chen, TC;Wu, CN;Hsu, JTA;Lee, JC;Hwang, MJ;Li, ML;Chen, GW;Hoc, MS
Contributors:	Division of Biotechnology and Pharmaceutical Research
Abstract:	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.
Keywords:	Medicine, Research & Experimental
Date:	2004
Relation:	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
Appears in Collections:	[John Tsu-An Hsu] Periodical Articles

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