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Molecular basis for the formation of ribonucleoprotein complex of crimean-congo hemorrhagic fever virus

文献类型：期刊论文

作者Wang, Xiaojing1; Li, Baobin2,3,10; Guo, Yu4,5,6; Shen, Shu7; Zhao, Liang1; Zhang, Peisheng2,3; Sun, Yuna6; Sui, Sen-Fang1; Deng, Fei7; Lou, Zhiyong2,3,4,5,8,9
刊名Journal of structural biology
出版日期2016-12-01
卷号196期号:3页码:455-465
ISSN号1047-8477
关键词Cchfv Nucleocapsid protein Oligomer Architecture
DOI10.1016/j.jsb.2016.09.013
通讯作者Sui, sen-fang(suisf@mail.tsinghua.edu.cn) ; Deng, fei(df@wh.iov.cn) ; Lou, zhiyong(louzy@mail.tsinghua.edu.cn)
英文摘要Negative-sense single-strand rna (-ssrna) viruses comprise a large family of pathogens that cause severe human infectious diseases. all-ssrna viruses encode a nucleocapsid protein (np) to encapsidate the viral genome, which, together with polymerase, forms a ribonucleoprotein complex (rnp) that is packaged into virions and acts as the template for viral replication and transcription. in our previous work, we solved the monomeric structure of np encoded by crimean-congo hemorrhagic fever virus (cchfv), which belongs to the nairovirus genus within the bunyaviridae family, and revealed its unusual endonuclease activity. however, the mechanism of cchfv rnp formation remains unclear, due to the difficulty in reconstructing the oligomeric cchfv np-rna complex. here, we identified and isolated the oligomeric cchfv np-rna complex that formed in expression cells. sequencing of rna extracted from the complex revealed sequence specificity and suggested a potential encapsidation signal facilitating the association between np and viral genome. a cryo-em reconstruction revealed the ring-shaped architecture of the cchfv np-rna oligomer, thus defining the interaction between the head and stalk domains that results in np multimerization. this structure also suggested a modified gating mechanism for viral genome encapsidation, in which both the head and stalk domains participate in rna binding. this work provides insight into the distinct mechanism underlying cchfv rnp formation compared to other ssrna viruses. (c) 2016 elsevier inc. all rights reserved.
WOS关键词NUCLEOPROTEIN-RNA COMPLEX ; EM STRUCTURE DETERMINATION ; NUCLEOCAPSID PROTEIN ; CRYSTAL-STRUCTURE ; ORTHOBUNYAVIRUS NUCLEOPROTEIN ; GENOME ENCAPSIDATION ; STRUCTURAL INSIGHTS ; ELECTRON-MICROSCOPY ; REVEALS ; MECHANISM
WOS研究方向Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
WOS类目Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
语种英语
出版者ACADEMIC PRESS INC ELSEVIER SCIENCE
WOS记录号WOS:000389295000018
URI标识http://www.irgrid.ac.cn/handle/1471x/2373488
专题武汉病毒研究所
通讯作者Sui, Sen-Fang; Deng, Fei; Lou, Zhiyong
作者单位1.Tsinghua Univ, Beijing Adv Innovat Ctr Struct Biol, Sch Life Sci, State Key Lab Biomembrane, Beijing 100084, Peoples R China
2.Tsinghua Univ, Sch Med, Beijing 100084, Peoples R China
3.Tsinghua Univ, MOE Lab Prot Sci, Beijing 100084, Peoples R China
4.Nankai Univ, Coll Pharm, Tianjin 300071, Peoples R China
5.Nankai Univ, State Key Lab Med Chem Biol, Tianjin 300071, Peoples R China
6.Chinese Acad Sci, Inst Biophys, Natl Lab Macromol, Beijing 100101, Peoples R China
7.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China
8.Sichuan Univ, State Key Lab Biotherapy, Chengdu 610041, Peoples R China
9.Sichuan Univ, Collaborat Innovat Ctr Biotherapy, West China Hosp, Chengdu 610041, Peoples R China
10.Univ Wisconsin, Sch Pharm, Madison, WI 53705 USA
推荐引用方式
GB/T 7714		 Wang, Xiaojing,Li, Baobin,Guo, Yu,et al. Molecular basis for the formation of ribonucleoprotein complex of crimean-congo hemorrhagic fever virus[J]. Journal of structural biology,2016,196(3):455-465.
APA Wang, Xiaojing.,Li, Baobin.,Guo, Yu.,Shen, Shu.,Zhao, Liang.,...&Lou, Zhiyong.(2016).Molecular basis for the formation of ribonucleoprotein complex of crimean-congo hemorrhagic fever virus.Journal of structural biology,196(3),455-465.
MLA Wang, Xiaojing,et al."Molecular basis for the formation of ribonucleoprotein complex of crimean-congo hemorrhagic fever virus".Journal of structural biology 196.3(2016):455-465.

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