Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus
文献类型:期刊论文
作者 | Wang, Zhao-Xi2,3,4,5,6,7; Liu, Shu-Bo2,7; Guan, Hongxin4,5,6; Lu, Long-Feng7; Tu, Jia-Gang3; Ouyang, Songying1,4,5,6; Zhang, Yong-An1,3,7 |
刊名 | JOURNAL OF VIROLOGY |
出版日期 | 2020-08-01 |
卷号 | 94期号:15页码:10 |
ISSN号 | 0022-538X |
关键词 | central domain crystal structure interferon negative regulator P protein SVCV |
DOI | 10.1128/JVI.00855-20 |
通讯作者 | Ouyang, Songying(ouyangsy@fjnu.edu.cn) ; Zhang, Yong-An(yonganzhang@mail.hzau.edu.cn) |
英文摘要 | Spring viremia of carp virus (SVCV) is a highly pathogenic Vesiculovirus in the common carp. The phosphoprotein (P protein) of SVCV is a multifunctional protein that acts as a polymerase cofactor and an antagonist of cellular interferon (IFN) response. Here, we report the 1.5-angstrom-resolution crystal structure of the P protein central domain (P-CD) of SVCV (SVCVPCD). The P-CD monomer consists of two beta sheets, an alpha helix, and another two beta sheets. Two P-CD monomers pack together through their hydrophobic surfaces to form a dimer. The mutations of residues on the hydrophobic surfaces of P-CD disrupt the dimer formation to different degrees and affect the expression of host IFN consistently. Therefore, the oligomeric state formation of the P protein of SVCV is an important mechanism to negatively regulate host IFN response. IMPORTANCE SVCV can cause spring viremia of carp with up to 90% lethality, and it is the homologous virus of the notorious vesicular stomatitis virus (VSV). There are currently no drugs that effectively cure this disease. P proteins of negative-strand RNA viruses (NSVs) play an essential role in many steps during the replication cycle and an additional role in immunosuppression as a cofactor. All P proteins of NSVs are oligomeric, but the studies on the role of this oligomerization mainly focus on the process of virus transcription or replication, and there are few studies on the role of P-CD in immunosuppression. Here, we present the crystal structure of SVCVPCD. A new mechanism of immune evasion is clarified by exploring the relationship between SVCVPCD and host IFN response from a structural biology point of view. These findings may provide more accurate target sites for drug design against SVCV and provide new insights into the function of NSVPCD. |
WOS关键词 | VESICULAR STOMATITIS-VIRUS ; P PROTEIN ; POLYMERASE COFACTOR ; CRYSTAL-STRUCTURE ; VP35 PROTEIN ; COMPLEX ; RNA ; PHOSPHORYLATION ; ACTIVATION ; MODEL |
资助项目 | National Natural Science Foundation of China[31725026] ; National Natural Science Foundation of China[31770948] ; National Natural Science Foundation of China[31570875] ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China[2018CFA011] ; Fujian Normal University[Z0210509] |
WOS研究方向 | Virology |
语种 | 英语 |
出版者 | AMER SOC MICROBIOLOGY |
WOS记录号 | WOS:000550173300007 |
资助机构 | National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Fujian Normal University ; Fujian Normal University ; Fujian Normal University ; Fujian Normal University ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Fujian Normal University ; Fujian Normal University ; Fujian Normal University ; Fujian Normal University ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Fujian Normal University ; Fujian Normal University ; Fujian Normal University ; Fujian Normal University ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Science Fund for Creative Research Groups of the Natural Science Foundation of Hubei Province of China ; Fujian Normal University ; Fujian Normal University ; Fujian Normal University ; Fujian Normal University |
源URL | [http://ir.ihb.ac.cn/handle/342005/38556] |
专题 | 水生生物研究所_水生生物分子与细胞生物学研究中心_期刊论文 |
通讯作者 | Ouyang, Songying; Zhang, Yong-An |
作者单位 | 1.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China 2.Univ Chinese Acad Sci, Beijing, Peoples R China 3.Huazhong Agr Univ, Coll Fisheries, State Key Lab Agr Microbiol, Wuhan, Peoples R China 4.Fujian Normal Univ, Coll Life Sci, Biomed Res Ctr South China, Key Lab Innate Immune Biol Fujian Prov, Fuzhou, Peoples R China 5.Fujian Normal Univ, Prov Univ Key Lab Cellular Stress Response & Meta, Coll Life Sci, Fuzhou, Peoples R China 6.Fujian Normal Univ, Coll Life Sci, Key Lab Optoelect Sci & Technol Med, Minist Educ, Fuzhou, Peoples R China 7.Chinese Acad Sci, Inst Hydrobiol, Wuhan, Peoples R China |
推荐引用方式 GB/T 7714 | Wang, Zhao-Xi,Liu, Shu-Bo,Guan, Hongxin,et al. Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus[J]. JOURNAL OF VIROLOGY,2020,94(15):10. |
APA | Wang, Zhao-Xi.,Liu, Shu-Bo.,Guan, Hongxin.,Lu, Long-Feng.,Tu, Jia-Gang.,...&Zhang, Yong-An.(2020).Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus.JOURNAL OF VIROLOGY,94(15),10. |
MLA | Wang, Zhao-Xi,et al."Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus".JOURNAL OF VIROLOGY 94.15(2020):10. |
入库方式: OAI收割
来源:水生生物研究所
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