Structure of the Leanyer orthobunyavirus nucleoprotein-RNA complex reveals unique architecture for RNA encapsidation

被引:52
|
作者
Niu, Fengfeng [1 ,2 ]
Shaw, Neil [1 ,3 ]
Wang, Yao E. [4 ]
Jiao, Lianying [1 ,2 ]
Ding, Wei [1 ]
Li, Xiaomin [1 ]
Zhu, Ping [1 ]
Upur, Halmurat [5 ]
Ouyang, Songying [1 ]
Cheng, Genhong [4 ]
Liu, Zhi-jie [1 ,3 ]
机构
[1] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[3] Kunming Med Univ, Inst Mol & Clin Med, Kunming 650500, Peoples R China
[4] Univ Calif Los Angeles, Dept Microbiol Immunol & Mol Genet, Los Angeles, CA 90095 USA
[5] Xinjiang Med Univ, Dept Drug Anal, Urumqi 830011, Xinjiang, Peoples R China
基金
中国国家自然科学基金;
关键词
crystal structure; nucleoprotein complex with ssRNA; RNP; VIRUS NUCLEOCAPSID PROTEIN; CRYSTAL-STRUCTURE; MACROMOLECULAR STRUCTURES; TRANSCRIPTION; DIFFRACTION; BINDING;
D O I
10.1073/pnas.1300035110
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Negative-stranded RNA viruses cover their genome with nucleoprotein (N) to protect it from the human innate immune system. Abrogation of the function of N offers a unique opportunity to combat the spread of the viruses. Here, we describe a unique fold of N from Leanyer virus (LEAV, Orthobunyavirus genus, Bunyaviridae family) in complex with single-stranded RNA refined to 2.78 angstrom resolution as well as a 2.68 angstrom resolution structure of LEAV N-ssDNA complex. LEAV N is made up of an N- and a C-terminal lobe, with the RNA binding site located at the junction of these lobes. The LEAV N tetramer binds a 44-nucleotide-long single-stranded RNA chain. Hence, oligomerization of N is essential for encapsidation of the entire genome and is accomplished by using extensions at the N and C terminus. Molecular details of the oligomerization of N are illustrated in the structure where a circular ring-like tertiary assembly of a tetramer of LEAV N is observed tethering the RNA in a positively charged cavity running along the inner edge. Hydrogen bonds between N and the C2 hydroxyl group of ribose sugar explain the specificity of LEAV N for RNA over DNA. In addition, base-specific hydrogen bonds suggest that some regions of RNA bind N more tightly than others. Hinge movements around F20 and V125 assist in the reversal of capsidation during transcription and replication of the virus. Electron microscopic images of the ribonucleoprotein complexes of LEAV N reveal a filamentous assembly similar to those found in phleboviruses.
引用
收藏
页码:9054 / 9059
页数:6
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