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Activation of NF-kB by the Full-length nucleocapsid protein of the SARS Coronavirus

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Acta Biochimica et Biophysica Sinica 2005年第9期37卷 607-612页

作者： Qing-Jiao LIAO Lin-Bai YE Khalid Amine TIMANI Ying-Chun ZENG Ying-Long SHE Li YE Zheng-Hui WU State Key Laboratory of Virology,College of Life Science,Wuhan University,Wuhan 430072,China State Key Laboratory of Virology College of Life Science Wuhan University Wuhan 430072 China.

The severe acute respiratory syndrome coronavirus (SARS-CoV) is the major causative agentfor the worldwide outbreak of SARS in *** mechanism by which SARS-CoV causes atypical pneu-monia remains *** nuclear factor kappa B (NF-kB) is a key transcription factor that activatesnumerous genes involved in cellular immune response and *** studies have shown that NF-kB plays an important role in the pathogenesis of lung *** this study,we investigated the possibleregulatory interaction between the SARS-CoV nucleocapsid (N) protein and NF-kB by luciferase *** results showed that the SARS-CoV N protein can significantly activate NF-kB only in Vero *** are susceptible to SARS-CoV infection,but not in Vero or HeLa *** suggests that NF-kBactivation is ***,NF-kB activation in Vero E6 cells expressing the N protein is *** experiments showed that there is more than one function domain in the N protein respon-sible for NF-kB *** data indicated the possible role of the N protein in the pathogenesis of SARS.

关键词： severe acute respiratory syndrome coronavirus (SARS-CoV) nucleocapsid protein NF-kB

Expression, Purification and Sublocalization of SARS-CoV nucleocapsid protein in Insect Cells

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Acta Biochimica et Biophysica Sinica 2004年第11期36卷 754-758页

作者： Ai-Xia REN, You-Hua XIE, Yu-Ying KONG, Guan-Zhen YANG, Yao-Zhou ZHANG,Yuan WANG, and Xiang-Fu WUInstitute of Biochemistry and Biotechnology, College of Life Science, Zhejiang University, Hangzhou 310029, China State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and cell Biology, Shanghai Institutes for Biological Sciences,Chinese Academy of Sciences, Graduate School of the Chinese Academy of Sciences, Shanghai 200031, China Institute of Biochemistry, Zhejiang University of Sciences, Hangzhou 310018, China Institute of Biochemistry and Biotechnology College of Life Science Zhejiang University Hangzhou 310029 China.

The causative agent of severe acute respiratory syndrome (SARS) is a previously unidentified coronavirus, SARS-CoV. The nucleocapsid (N) protein of SARS-CoV is a major viral protein recognized by acute and early convalescent sera from SARS patients. To facilitate the studies on the function and structure of the N protein, this report describe the expression and purification of recombinant SARS-CoV N protein using the baculovirus

关键词： severe acute respiratory syndrome (SARS) SARS coronavirus nucleocapsid protein baculovirus insect cells

Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirus

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protein & Cell 2010年第7期1卷 688-697页

作者： Yanlin Ma Xiaohang Tong Xiaoling Xu Xuemei Li Zhiyong Lou Zihe Rao Life National Laboratory of Biomacromolecules Institute of BiophysicsChinese Academy of SciencesBeijing 100101China Graduate University of the Chinese Academy of Sciences Beijing 100049China Laboratory of Structural Biology Tsinghua UniversityBeijing 100084China

Coronaviruses are the causative agent of respiratory and enteric diseases in animals and *** example is SARS,which caused a worldwide health threat in *** coronaviruses,the structural protein N(nucleocapsid protein)associates with the viral RNA to form the filamentous nucleocapsid and plays a crucial role in genome replication and *** structure of Nterminal domain of MHV N protein also implicated its specific affinity with transcriptional regulatory sequence(TRS)*** we report the crystal structures of the two proteolytically resistant N-(NTD)and C-terminal(CTD)domains of the N protein from murine hepatitis virus(MHV).The structure of NTD in two different crystal forms was solved to 1.5Å.The higher resolution provides more detailed structural information than previous reports,showing that the NTD structure from MHV shares a similar overall and topology structure with that of SARS-CoV and IBV,but varies in its potential surface,which indicates a possible difference in RNA-binding *** structure of CTD was solved to 2.0-Åresolution and revealed a tightly intertwined *** is consistent with analytical ultracentrifugation experiments,suggesting a dimeric assembly of the N *** similarity between the structures of these two domains from SARS-CoV,IBV and MHV corroborates a conserved mechanism of nucleocapsid formation for coronaviruses.

关键词： crystal structure nucleocapsid protein murine hepatitis virus

Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites

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Acta Pharmaceutica Sinica B 2020年第7期10卷 1228-1238页

作者： Sisi Kang Mei Yang Zhongsi Hong Liping Zhang Zhaoxia Huang Xiaoxue Chen Suhua He Ziliang Zhou Zhechong Zhou Qiuyue Chen Yan Yan Changsheng Zhang Hong Shan Shoudeng Chen Molecular Imaging Center Guangdong Provincial Key Laboratory of Biomedical Imagingthe Fifth Affiliated HospitalSun Yat-sen UniversityZhuhai 519000China Department of Infectious Diseases the Fifth Affiliated HospitalSun Yat-sen UniversityZhuhai 519000China Key Laboratory of Tropical Marine Bio-resources and Ecology Guangdong Key Laboratory of Marine Materia MedicaInstitution of South China Sea Ecology and Environmental EngineeringSouth China Sea Institute of OceanologyChinese Academy of SciencesGuangzhou 510301China Guangdong Provincial Engineering Research Center of Molecular Imaging the Fifth Affiliated HospitalSun Yatsen UniversityZhuhai 519000China Department of Interventional Medicine the Fifth Affiliated HospitalSun Yat-sen UniversityZhuhai 519000China Department of Experimental Medicine the Fifth Affiliated HospitalSun Yat-sen UniversityZhuhai 519000China

The outbreak of coronavirus disease(COVID-19)caused by SARS-CoV-2 virus continually lead to worldwide human infections and ***,there is no specific viral protein-targeted *** nucleocapsid protein is a potential antiviral drug target,serving multiple critical functions during the viral life ***,the structural information of SARS-CoV-2 nucleocapsid protein remains ***,we have determined the 2.7 A crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 nucleocapsid *** the overall structure is similar as other reported coronavirus nucleocapsid protein N-terminal domain,the surface electrostatic potential characteristics between them are *** comparison with mild virus type HCoV-OC43 equivalent domain demonstrates a unique potential RNA binding pocket alongside theβ-sheet *** by in vitro binding studies,our data provide several atomic resolution features of SARS-CoV-2 nucleocapsid protein N-terminal domain,guiding the design of novel antiviral agents specific targeting to SARS-CoV-2.

关键词： COVID-19 Coronavirus SARS-CoV-2 nucleocapsid protein RNA binding domain Crystal structure Antiviral targeting site

The nucleocapsid protein of rice stripe virus in cell nuclei of vector insect regulates viral replication

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protein & Cell 2022年第5期13卷 360-378页

作者： Wan Zhao Junjie Zhu Hong Lu Jiaming Zhu Fei Jiang Wei Wang Lan Luo Le Kang Feng Cui State Key Laboratory of Integrated Management of Pest Insects and Rodents Institute of ZoologyChinese Academy of SciencesBeijing 100101China CAS Center for Excellence in Biotic Interactions University of Chinese Academy of SciencesBeijing 100049China

Rice stripe virus(RSV)transmitted by the small brown planthopper causes severe rice yield losses in Asian *** viral nuclear entry promotes viral replication in host cells,whether this phenomenon occurs in vector cells remains ***,in this study,we systematically evaluated the presence and roles of RSV in the nuclei of vector insect *** observed that the nucleocapsid protein(NP)and viral genomic RNAs were partially transported into vector cell nuclei by utilizing the importin a nuclear transport *** blocking NP nuclear localization,cytoplasmic RSV accumulation significantly *** the vector cell nuclei,NP bound the transcription factor YY1 and affected its positive regulation to ***,decreased FAIM expression triggered an antiviral caspase-dependent apoptotic *** results reveal that viral nuclear entry induces completely different immune effects in vector and host cells,providing new insights into the balance between viral load and the immunity pressure in vector insects.

关键词： rice stripe virus nucleocapsid protein nuclear localization importinα YY1

nucleocapsid protein from porcine epidemic diarrhea virus isolates can antagonize interferon-λ production by blocking the nuclear factor-κB nuclear translocation

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Journal of Zhejiang University-Science B(Biomedicine & Biotechnology) 2018年第7期19卷 570-580页

作者： Ying SHAN Zi-qi LIU Guo-wei LI Cong CHEN Hao LUO Ya-jie LIU Xun-hui ZHUO Xing-fen SHI Wei-huan FANG Xiao-liang LI Zhejiang Province Key Lab of Preventive Veterinary Medicine Institute of Preventive Veterainary Medicine College of Animal Sciences Zhejiang University Hangzhou 310058 China Institute of Parasitic Disease Zhejiang Academy of Medical Sciences Hangzhou 310013 China Animal Products Quality Testing Center of Zhejiang Province Hangzhou 310020 China

Porcine epidemic diarrhea virus（PEDV） is a highly infectious pathogen that can cause severe diseases in pigs and result in enormous economic losses in the worldwide swine industry. Previous studies revealed that PEDV exhibits an obvious capacity for modulating interferon（IFN） signaling or expression. The newly discovered type III IFN, which plays a crucial role in antiviral immunity, has strong antiviral activity against PEDV proliferation in IPEC-J2 cells. In this study, we aimed to investigate the effect of PEDV nucleocapsid（N） protein on type III IFN-λ. We found that the N proteins of ten PEDV strains isolated between 2013 and 2017 from different local farms shared high nucleotide identities, while the N protein of the CV777 vaccine strain formed a monophyletic branch in the phylogenetic tree. The N protein of the epidemic strain could antagonize type III IFN, but not type I or type II IFN expression induced by polyinosinic-polycytidylic acid（poly（I：C）） in IPEC-J2 cells. Subsequently, we demonstrated that the inhibition of poly（I：C）-induced IFN-λ3 production by PEDV N protein was dependent on the blocking of nuclear factor-κB（NF-κB） nuclear translocation. These findings might help increase understanding of the pathogenesis of PEDV and its mechanisms for evading the host immune response.

关键词： Porcine epidemic diarrhea virus nucleocapsid protein Interferon-λ(IFN-λ) Nuclear factor-κB(NF-κB) Intestinal epithelial cells

Indirect Enzyme-Linked Immunosorbent Assay Based on the nucleocapsid protein of SARS-like Coronaviruses

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Virologica Sinica 2009年第2期24卷 146-151页

作者： Jun-fa YUAN Yan LI Hua-jun ZHANG Peng ZHOU Zhen-hua KE Yun-zhi ZHANG Zheng-li SHI Wuhan Institute of Virology Chinese Academy of Sciences Wuhan 430071 China Yunnan Institute ofEndemic Diseases Control and Prevention Dali 671000 China

The nucleocapsid protein(N) is a major structural protein of coronaviruses. The N protein of bat SARS-like coronavirus(SL-CoV) has a high similarity with that of SARS-CoV. In this study,the SL-CoV N protein was expressed in Escherichia coli,purified and used as antigen. An Indirect Enzyme-Linked Immunosorbent Assay(indirect ELISA) was developed for detection of SARS-or SL-CoV infections in bat populations. The detection of 573 bat sera with this indirect ELISA demonstrated that SL-CoVs consistently circulate in Rhinilophus species,further supporting the proposal that bats are natural reservoirs of SL-CoVs. This method uses 1-2 μl of serum sample and can be used for preliminary screening of infections by SARS-or SL-CoV with a small amount of serum sample.

关键词： SARS-like CoV nucleocapsid protein Indirect ELISA

The Epitope Study on the SARS-CoV nucleocapsid protein

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Genomics, Proteomics & Bioinformatics 2003年第3期1卷 198-206页

作者： Shuting Li, Liang Lin, Hao Wang, Jianning Yin, Yan Ren, Zhe Zhao, Jie Wen, Cuiqi Zhou, Xumin Zhang, Xiaolei Li, Jingqiang Wang, Zhengfeng Zhou, Jinxiu Liu, Jianmin Shao, Tingting Lei, Jianqiu Fang, Ningzhi Xu, and Siqi LiuBeijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China & Beijing Proteomics Institute, Beijing 101300, China Beijing Genomics Institute Chinese Academy of Sciences Beijing 101300 China.

The nucleocapsid protein (N protein) has been found to be an antigenic protein in a number of coronaviruses. Whether the N protein in severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is antigenic remains to be elucidated. Using Western blot and Enzyme-linked Immunosorbent Assay (ELISA), the recombinant N proteins and the synthesized peptides derived from the N protein were screened in sera from SARS patients. All patient sera in this study displayed strong positive immunoreactivities against the recombinant N proteins, whereas normal sera gave negative immunoresponses to these proteins, indicating that the N protein of SARS-CoV is an antigenic protein. Furthermore, the epitope sites in the N protein were determined by competition experiments, in which the recombinant proteins or the synthesized peptides competed against the SARS-CoV proteins to bind to the antibodies raised in SARS sera. One epitope site located at the C-terminus was confirmed as the most antigenic region in this protein. A detailed screening of peptide with ELISA demonstrated that the amino sequence from Codons 371 to 407 was the epitope site at the C-terminus of the N protein. Understanding of the epitope sites could be very significant for developing an effective diagnostic approach to SARS.

关键词： SARS coronavirus nucleocapsid protein antigenicity epitope

The C-Terminal Portion of the nucleocapsid protein Demonstrates SARS-CoV Antigenicity

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Genomics, Proteomics & Bioinformatics 2003年第3期1卷 193-197页

作者： GuozhenLiu ShaohuiHu YongwuHu PengChen JianningYin JieWen JingqiangWang[ LiangLin JinxiuLiu BoYou YeYin ShutingLi HaoWang YanRen JiaJi XiaoqianZhao YongqiaoSun XiaoweiZhang JianqiuFang JianWang SiqiLiu JunYu HengZhu HuanmingYang CollegeofLifeSciences HebeiAgriculturalUniversityBaoding071001China BeijingGenomicsInstitute ChineseAcademyofSciencesBeijing101300China WenzhouMedicalCollege Wenzhou325007China Molecular CellularandDevelopmentalBiologyYaleUniversityCT06520U.S.A.

In order to develop clinical diagnostic tools for rapid detection of SARS-CoV (severe acute respiratory syndrome-associated coronavirus) and to identify candidate proteins for vaccine development, the C-terminal portion of the nucleocapsid (NC) gene was amplified using RT-PCR from the SARS-CoV genome, cloned into a yeast expression vector (pEGH), and expressed as a glutathione S-transferase (GST) and Hisx6 double-tagged fusion protein under the control of an inducible promoter. Western analysis on the purified protein confirmed the expression and purification of the NC fusion proteins from yeast. To determine its antigenicity, the fusion protein was challenged with serum samples from SARS patients and normal controls. The NC fusion protein demonstrated high antigenicity with high specificity, and therefore, it should have great potential in designing clinical diagnostic tools and provide useful information for vaccine development.

关键词： Severe Acute Respiratory Syndrome (SARS) coronavirus nucleocapsid protein antigenicity yeast expression system