• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

瘟病毒多聚蛋白的加工:经典猪瘟病毒自身蛋白酶与核衣壳蛋白之间的切割位点

Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus.

作者信息

Stark R, Meyers G, Rümenapf T, Thiel H J

机构信息

Federal Research Centre for Virus Diseases of Animals, Tübingen, Federal Republic of Germany.

出版信息

J Virol. 1993 Dec;67(12):7088-95. doi: 10.1128/JVI.67.12.7088-7095.1993.

DOI:10.1128/JVI.67.12.7088-7095.1993
PMID:8230432
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC238170/
Abstract

The polyprotein of classical swine fever virus starts with the nonstructural protein p23, which is followed by the nucleocapsid protein p14. Proteolytic cleavage between p23 and p14 was demonstrated in a cell-free transcription-translation system. Successive truncation of the cDNA used for the transcription indicated that the proteolytic activity responsible for the cleavage between p23 and p14 resides within p23. In order to determine the cleavage site between these two proteins, the respective genomic regions were expressed in two different expression systems. N-terminal sequencing of the resulting p14-related proteins revealed that cleavage occurs between Cys-168 and Ser-169. Comparison of the sequence around the cleavage site with sequences of other pestiviruses suggests a conserved processing site between similar proteins.

摘要

经典猪瘟病毒的多聚蛋白起始于非结构蛋白p23,随后是核衣壳蛋白p14。在无细胞转录-翻译系统中证实了p23和p14之间的蛋白水解切割。用于转录的cDNA的连续截短表明,负责p23和p14之间切割的蛋白水解活性存在于p23内。为了确定这两种蛋白之间的切割位点,在两种不同的表达系统中表达了各自的基因组区域。对所得p14相关蛋白的N端测序表明,切割发生在Cys-168和Ser-169之间。将切割位点周围的序列与其他瘟病毒的序列进行比较,提示相似蛋白之间存在保守的加工位点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/446f/238170/66e2eca8fa6a/jvirol00033-0190-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/446f/238170/12051626e6bd/jvirol00033-0188-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/446f/238170/76112573b050/jvirol00033-0189-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/446f/238170/487ba28ed2af/jvirol00033-0189-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/446f/238170/66e2eca8fa6a/jvirol00033-0190-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/446f/238170/12051626e6bd/jvirol00033-0188-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/446f/238170/76112573b050/jvirol00033-0189-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/446f/238170/487ba28ed2af/jvirol00033-0189-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/446f/238170/66e2eca8fa6a/jvirol00033-0190-a.jpg

相似文献

1
Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus.瘟病毒多聚蛋白的加工:经典猪瘟病毒自身蛋白酶与核衣壳蛋白之间的切割位点
J Virol. 1993 Dec;67(12):7088-95. doi: 10.1128/JVI.67.12.7088-7095.1993.
2
Processing of the envelope glycoproteins of pestiviruses.瘟病毒包膜糖蛋白的加工过程。
J Virol. 1993 Jun;67(6):3288-94. doi: 10.1128/JVI.67.6.3288-3294.1993.
3
Determination of Critical Requirements for Classical Swine Fever Virus NS2-3-Independent Virion Formation.测定猪瘟病毒 NS2-3 非依赖性病毒粒子形成的关键要求。
J Virol. 2019 Aug 28;93(18). doi: 10.1128/JVI.00679-19. Print 2019 Sep 15.
4
Expression and identification of hepatitis C virus polyprotein cleavage products.丙型肝炎病毒多聚蛋白裂解产物的表达与鉴定
J Virol. 1993 Mar;67(3):1385-95. doi: 10.1128/JVI.67.3.1385-1395.1993.
5
Cloning, expression and sequence analysis of the classical swine fever virus nucleocapsid protein.经典猪瘟病毒核衣壳蛋白的克隆、表达及序列分析
Virus Genes. 1998;16(2):225-34. doi: 10.1023/a:1007976208935.
6
Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis.南安普敦病毒中的多聚蛋白加工:通过体外诱变鉴定3C样蛋白酶切割位点
J Virol. 1996 Apr;70(4):2605-10. doi: 10.1128/JVI.70.4.2605-2610.1996.
7
Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein.有证据表明,黄热病毒非结构蛋白NS3的N端结构域是一种丝氨酸蛋白酶,负责病毒多聚蛋白的位点特异性切割。
Proc Natl Acad Sci U S A. 1990 Nov;87(22):8898-902. doi: 10.1073/pnas.87.22.8898.
8
Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.负责非结构多蛋白自催化加工的猫杯状病毒蛋白酶的定位以及一种稳定的蛋白酶 - 聚合酶前体蛋白的鉴定。
J Virol. 1999 Aug;73(8):6626-33. doi: 10.1128/JVI.73.8.6626-6633.1999.
9
Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites.丙型肝炎病毒编码的丝氨酸蛋白酶的特性:蛋白酶依赖性多蛋白切割位点的确定。
J Virol. 1993 May;67(5):2832-43. doi: 10.1128/JVI.67.5.2832-2843.1993.
10
In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids.西尼罗河病毒蛋白的体外合成表明,NS3蛋白的氨基末端片段包含蛋白酶的活性中心,该蛋白酶在多个碱性氨基酸之后切割病毒多聚蛋白。
J Gen Virol. 1991 Apr;72 ( Pt 4):851-8. doi: 10.1099/0022-1317-72-4-851.

引用本文的文献

1
Mapping evolutionary paradigm of bovine viral diarrhea virus associated with different organizations of nucleotide.绘制与不同核苷酸组织相关的牛病毒性腹泻病毒的进化模式
Virulence. 2025 Dec;16(1):2550620. doi: 10.1080/21505594.2025.2550620. Epub 2025 Aug 29.
2
N-terminal domain of classical swine fever virus N induces proteasomal degradation of specificity protein 1 with reduced HDAC1 expression to evade from innate immune responses.经典猪瘟病毒N蛋白的N端结构域诱导特异性蛋白1的蛋白酶体降解,同时降低组蛋白去乙酰化酶1的表达,以逃避天然免疫反应。
J Virol. 2023 Oct 31;97(10):e0111523. doi: 10.1128/jvi.01115-23. Epub 2023 Oct 5.
3

本文引用的文献

1
Bovine viral diarrhea virus genomic organization.牛病毒性腹泻病毒基因组结构
Arch Virol Suppl. 1991;3:19-27. doi: 10.1007/978-3-7091-9153-8_3.
2
Processing of the envelope glycoproteins of pestiviruses.瘟病毒包膜糖蛋白的加工过程。
J Virol. 1993 Jun;67(6):3288-94. doi: 10.1128/JVI.67.6.3288-3294.1993.
3
Use of protein A-bearing staphylococci for the immunoprecipitation and isolation of antigens from cells.利用携带蛋白A的葡萄球菌从细胞中免疫沉淀和分离抗原。
Attachment, Entry, and Intracellular Trafficking of Classical Swine Fever Virus.
经典猪瘟病毒的附着、进入和细胞内运输。
Viruses. 2023 Sep 3;15(9):1870. doi: 10.3390/v15091870.
4
A Genetically Engineered Bivalent Vaccine Coexpressing a Molecular Adjuvant against Classical Swine Fever and Porcine Epidemic Diarrhea.一种表达针对经典猪瘟和猪流行性腹泻的分子佐剂的基因工程二价疫苗。
Int J Mol Sci. 2023 Jul 26;24(15):11954. doi: 10.3390/ijms241511954.
5
Different Types of Vaccines against Pestiviral Infections: "Barriers" for "".针对黄病毒感染的不同类型疫苗:“障碍”为“”。
Viruses. 2022 Dec 20;15(1):2. doi: 10.3390/v15010002.
6
Genetic characterization of atypical porcine pestivirus from neonatal piglets with congenital tremor in Hubei province, China.中国湖北省先天性震颤仔猪中一种非典型猪瘟病毒的遗传特征。
Virol J. 2022 Mar 24;19(1):51. doi: 10.1186/s12985-022-01780-8.
7
Fc-Mediated E2-Dimer Subunit Vaccines of Atypical Porcine Pestivirus Induce Efficient Humoral and Cellular Immune Responses in Piglets.Fc 介导的非典型猪瘟病毒 E2 二聚体亚单位疫苗可诱导仔猪产生有效的体液和细胞免疫应答。
Viruses. 2021 Dec 6;13(12):2443. doi: 10.3390/v13122443.
8
Genetic diversity and detection of atypical porcine pestivirus infections.遗传多样性和非典型猪瘟病毒感染的检测。
J Anim Sci. 2022 Jan 1;100(1). doi: 10.1093/jas/skab360.
9
PROFICS: A bacterial selection system for directed evolution of proteases.PROFICS:一种用于定向进化蛋白酶的细菌选择系统。
J Biol Chem. 2021 Oct;297(4):101095. doi: 10.1016/j.jbc.2021.101095. Epub 2021 Aug 19.
10
Membrane Topology of Pestiviral Non-Structural Protein 2 and determination of the minimal autoprotease domain.瘟病毒非结构蛋白2的膜拓扑结构及最小自蛋白酶结构域的确定
J Virol. 2021 May 10;95(11). doi: 10.1128/JVI.00154-21. Epub 2021 Mar 17.
Methods Enzymol. 1981;73(Pt B):442-59. doi: 10.1016/0076-6879(81)73084-2.
4
C-type particles produced by a permanent cell line from a leukemic pig. I. Origin and properties of the host cells and some evidence for the occurrence of C-type-like particles.一株白血病猪的永久细胞系产生的C型颗粒。I. 宿主细胞的起源和特性以及C型样颗粒存在的一些证据。
Virology. 1974 Jan;57(1):175-8. doi: 10.1016/0042-6822(74)90118-4.
5
Characterization of foot-and-mouth disease virus gene products with antisera against bacterially synthesized fusion proteins.用针对细菌合成融合蛋白的抗血清对口蹄疫病毒基因产物进行特性鉴定。
J Virol. 1986 Mar;57(3):983-91. doi: 10.1128/JVI.57.3.983-991.1986.
6
Proteins encoded by bovine viral diarrhea virus: the genomic organization of a pestivirus.牛病毒性腹泻病毒编码的蛋白质:瘟病毒的基因组结构
Virology. 1988 Jul;165(1):200-8. doi: 10.1016/0042-6822(88)90673-3.
7
Molecular cloning and nucleotide sequence of the pestivirus bovine viral diarrhea virus.瘟病毒属牛病毒性腹泻病毒的分子克隆与核苷酸序列
Virology. 1988 Jul;165(1):191-9. doi: 10.1016/0042-6822(88)90672-1.
8
Molecular cloning and nucleotide sequence of the genome of hog cholera virus.猪霍乱病毒基因组的分子克隆与核苷酸序列
Virology. 1989 Aug;171(2):555-67. doi: 10.1016/0042-6822(89)90625-9.
9
Hog cholera virus--characterization of specific antiserum and identification of cDNA clones.
Virology. 1989 Jul;171(1):18-27. doi: 10.1016/0042-6822(89)90506-0.
10
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.用于分离1至100 kDa范围内蛋白质的三羟甲基氨基甲烷-十二烷基硫酸钠-聚丙烯酰胺凝胶电泳
Anal Biochem. 1987 Nov 1;166(2):368-79. doi: 10.1016/0003-2697(87)90587-2.