Short peptides derived from the interaction domain of SARS coronavirus nonstructural protein nsp10 can suppress the 2′-O-methyltransferase activity of nsp10/nsp16 complex

被引:61
作者
Ke, Min [1 ,2 ]
Chen, Yu [1 ,2 ]
Wu, Andong [1 ,2 ]
Sun, Ying [1 ,2 ]
Su, Ceyang [1 ,2 ]
Wu, Hao [1 ,2 ]
Jin, Xu [1 ,2 ]
Tao, Jiali [1 ,2 ]
Wang, Yi [1 ,2 ]
Ma, Xiao [1 ,2 ]
Pan, Ji-An [1 ,2 ]
Guo, Deyin [1 ,2 ]
机构
[1] Wuhan Univ, Coll Life Sci, State Key Lab Virol, Wuhan 430072, Peoples R China
[2] Wuhan Univ, Coll Life Sci, Modern Virol Res Ctr, Wuhan 430072, Peoples R China
关键词
SARS; Coronavirus; nsp10; nsp16; 2 '-O-methyltransferase; Peptides; ACUTE RESPIRATORY SYNDROME; METHYLTRANSFERASE; EXORIBONUCLEASE; REPLICATION; INHIBITORS; THERAPIES; REVEALS; GENOME; TARGET; VIRUS;
D O I
10.1016/j.virusres.2012.05.017
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Coronaviruses are the etiological agents of respiratory and enteric diseases in humans and livestock, exemplified by the life-threatening severe acute respiratory syndrome (SARS) caused by SARS coronavirus (SARS-CoV). However, effective means for combating coronaviruses are still lacking. The interaction between nonstructural protein (nsp) 10 and nsp16 has been demonstrated and the crystal structure of SARS-CoV nsp16/10 complex has been revealed. As nsp10 acts as an essential trigger to activate the 2'-O-methyltransferase activity of nsp16, short peptides derived from nsp10 may have inhibitory effect on viral 2'-O-methyltransferase activity. In this study, we revealed that the domain of aa 65-107 of nsp10 was sufficient for its interaction with nsp16 and the region of aa 42-120 in nsp10, which is larger than the interaction domain, was needed for stimulating the nsp16 2'-O-methyltransferase activity. We further showed that two short peptides derived from the interaction domain of nsp10 could inhibit the 2'-O-methyltransferase activity of SARS-CoV nsp16/10 complex, thus providing a novel strategy and proof-of-principle study for developing peptide inhibitors against SARS-CoV. (c) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:322 / 328
页数:7
相关论文
共 28 条
[1]   Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities [J].
Ahola, T ;
Laakkonen, P ;
Vihinen, H ;
Kaariainen, L .
JOURNAL OF VIROLOGY, 1997, 71 (01) :392-397
[2]   Update on SARS research and other possibly zoonotic coronaviruses [J].
Anderson, Larry J. ;
Tong, Suxiang .
INTERNATIONAL JOURNAL OF ANTIMICROBIAL AGENTS, 2010, 36 :S21-S25
[3]   In Vitro Reconstitution of SARS-Coronavirus mRNA Cap Methylation [J].
Bouvet, Mickael ;
Debarnot, Claire ;
Imbert, Isabelle ;
Selisko, Barbara ;
Snijder, Eric J. ;
Canard, Bruno ;
Decroly, Etienne .
PLOS PATHOGENS, 2010, 6 (04) :1-13
[4]  
Chen P, 2007, J BIOCHEM MOL BIOL, V40, P649
[5]   Biochemical and Structural Insights into the Mechanisms of SARS Coronavirus RNA Ribose 2′-O-Methylation by nsp16/nsp10 Protein Complex [J].
Chen, Yu ;
Su, Ceyang ;
Ke, Min ;
Jin, Xu ;
Xu, Lirong ;
Zhang, Zhou ;
Wu, Andong ;
Sun, Ying ;
Yang, Zhouning ;
Tien, Po ;
Ahola, Tero ;
Liang, Yi ;
Liu, Xinqi ;
Guo, Deyin .
PLOS PATHOGENS, 2011, 7 (10)
[6]   Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase [J].
Chen, Yu ;
Cai, Hui ;
Pan, Ji'an ;
Xiang, Nian ;
Tien, Po ;
Ahola, Tero ;
Guo, Deyin .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2009, 106 (09) :3484-3489
[7]   2′-O methylation of the viral mRNA cap evades host restriction by IFIT family members [J].
Daffis, Stephane ;
Szretter, Kristy J. ;
Schriewer, Jill ;
Li, Jianqing ;
Youn, Soonjeon ;
Errett, John ;
Lin, Tsai-Yu ;
Schneller, Stewart ;
Zust, Roland ;
Dong, Hongping ;
Thiel, Volker ;
Sen, Ganes C. ;
Fensterl, Volker ;
Klimstra, William B. ;
Pierson, Theodore C. ;
Buller, R. Mark ;
Gale, Michael, Jr. ;
Shi, Pei-Yong ;
Diamond, Michael S. .
NATURE, 2010, 468 (7322) :452-456
[8]   Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex [J].
Debarnot, Claire ;
Imbert, Isabelle ;
Ferron, Francois ;
Gluais, Laure ;
Varlet, Isabelle ;
Papageorgiou, Nicolas ;
Bouvet, Mickael ;
Lescar, Julien ;
Decroly, Etienne ;
Canard, Bruno .
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2011, 67 :404-408
[9]   Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2'O)-methyltransferase activity [J].
Decroly, Etienne ;
Imbert, Isabelle ;
Coutard, Bruno ;
Bouvet, Mickael ;
Selisko, Barbara ;
Alvarez, Karine ;
Gorbalenya, Alexander E. ;
Snijder, Eric J. ;
Canard, Bruno .
JOURNAL OF VIROLOGY, 2008, 82 (16) :8071-8084
[10]   Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex [J].
Decroly, Etienne ;
Debarnot, Claire ;
Ferron, Francois ;
Bouvet, Mickael ;
Coutard, Bruno ;
Imbert, Isabelle ;
Gluais, Laure ;
Papageorgiou, Nicolas ;
Sharff, Andrew ;
Bricogne, Gerard ;
Ortiz-Lombardia, Miguel ;
Lescar, Julien ;
Canard, Bruno .
PLOS PATHOGENS, 2011, 7 (05)