• 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

蛋白 F9 的 2.1 Å 结构及其与 L1 的比较，L1 是保守痘病毒进入-融合复合物的两个组成部分之一。

The 2.1 Å structure of protein F9 and its comparison to L1, two components of the conserved poxvirus entry-fusion complex.

机构信息

Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA.

Structural Biology Section, Research Technologies Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, Maryland, USA.

出版信息

Sci Rep. 2018 Nov 14;8(1):16807. doi: 10.1038/s41598-018-34244-7.

DOI:10.1038/s41598-018-34244-7
PMID:30429486
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6235832/
Abstract

The poxvirus F9 protein is a component of the vaccinia virus entry fusion complex (EFC) which consists of 11 proteins. The EFC forms a unique apparatus among viral fusion proteins and complexes. We solved the atomic structure of the F9 ectodomain at 2.10 Å. A structural comparison to the ectodomain of the EFC protein L1 indicated a similar fold and organization, in which a bundle of five α-helices is packed against two pairs of β-strands. However, instead of the L1 myristoylation site and hydrophobic cavity, F9 possesses a protruding loop between α-helices α3 and α4 starting at Gly90. Gly90 is conserved in all poxviruses except Salmon gill poxvirus (SGPV) and Diachasmimorpha longicaudata entomopoxvirus. Phylogenetic sequence analysis of all Poxviridae F9 and L1 orthologs revealed the SGPV genome to contain the most distantly related F9 and L1 sequences compared to the vaccinia proteins studied here. The structural differences between F9 and L1 suggest functional adaptations during evolution from a common precursor that underlie the present requirement for each protein.

摘要

痘病毒 F9 蛋白是构成包含 11 种蛋白的牛痘病毒进入融合复合物（EFC）的一个组成部分。EFC 在病毒融合蛋白和复合物中形成一种独特的装置。我们以 2.10Å 的分辨率解析了 F9 胞外域的原子结构。与 EFC 蛋白 L1 的胞外域的结构比较表明，两者具有相似的折叠和结构组织，其中五束α-螺旋与两对β-折叠相对排列。然而，F9 具有 Gly90 起始的α3 和α4 之间的突出环，而不是 L1 的豆蔻酰化位点和疏水性腔。除了鲑鱼鳃痘病毒（SGPV）和长尾鳞翅目昆虫痘病毒外，所有痘病毒都具有 Gly90。对所有痘病毒科 F9 和 L1 直系同源物的系统发育序列分析表明，与这里研究的牛痘病毒蛋白相比，SGPV 基因组包含最远距离相关的 F9 和 L1 序列。F9 和 L1 之间的结构差异表明，在从共同前体进化过程中发生了功能适应，这是目前对每种蛋白的要求的基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/f7afb005e761/41598_2018_34244_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/172d1fd01b93/41598_2018_34244_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/a98f01476557/41598_2018_34244_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/0906b1dda5f8/41598_2018_34244_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/9cbf31bac164/41598_2018_34244_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/c33e3a897219/41598_2018_34244_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/f7afb005e761/41598_2018_34244_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/172d1fd01b93/41598_2018_34244_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/a98f01476557/41598_2018_34244_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/0906b1dda5f8/41598_2018_34244_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/9cbf31bac164/41598_2018_34244_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/c33e3a897219/41598_2018_34244_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e62/6235832/f7afb005e761/41598_2018_34244_Fig6_HTML.jpg

相似文献

1
The 2.1 Å structure of protein F9 and its comparison to L1, two components of the conserved poxvirus entry-fusion complex.蛋白 F9 的 2.1 Å 结构及其与 L1 的比较，L1 是保守痘病毒进入-融合复合物的两个组成部分之一。
Sci Rep. 2018 Nov 14;8(1):16807. doi: 10.1038/s41598-018-34244-7.
2
Mutations Near the N Terminus of Vaccinia Virus G9 Protein Overcome Restrictions on Cell Entry and Syncytium Formation Imposed by the A56/K2 Fusion Regulatory Complex.痘苗病毒 G9 蛋白 N 端附近的突变克服了 A56/K2 融合调节复合物对细胞进入和合胞体形成的限制。
J Virol. 2020 May 4;94(10). doi: 10.1128/JVI.00077-20.
3
NMR assignments of vaccinia virus protein A28: an entry-fusion complex component.牛痘病毒蛋白 A28 的 NMR 结构解析：一种进入融合复合物的组成成分。
Biomol NMR Assign. 2021 Apr;15(1):117-120. doi: 10.1007/s12104-020-09993-0. Epub 2021 Jan 4.
4
Vaccinia virus F9 virion membrane protein is required for entry but not virus assembly, in contrast to the related L1 protein.与相关的L1蛋白不同，痘苗病毒F9病毒粒子膜蛋白是病毒进入所必需的，但不是病毒组装所必需的。
J Virol. 2006 Oct;80(19):9455-64. doi: 10.1128/JVI.01149-06.
5
Insights into the Organization of the Poxvirus Multicomponent Entry-Fusion Complex from Proximity Analyses in Living Infected Cells.活感染细胞的邻近分析揭示痘病毒多成分进入融合复合物的组织。
J Virol. 2021 Jul 26;95(16):e0085221. doi: 10.1128/JVI.00852-21.
6
Membrane fusion during poxvirus entry.痘病毒进入过程中的膜融合
Semin Cell Dev Biol. 2016 Dec;60:89-96. doi: 10.1016/j.semcdb.2016.07.015. Epub 2016 Jul 14.
7
Vaccinia virus l1 protein is required for cell entry and membrane fusion.痘苗病毒L1蛋白是细胞进入和膜融合所必需的。
J Virol. 2008 Sep;82(17):8687-94. doi: 10.1128/JVI.00852-08. Epub 2008 Jul 2.
8
Characterization of a newly identified 35-amino-acid component of the vaccinia virus entry/fusion complex conserved in all chordopoxviruses.痘苗病毒进入/融合复合体中一个新鉴定的35个氨基酸组成部分的特征，该组成部分在所有脊索痘病毒中保守。
J Virol. 2009 Dec;83(24):12822-32. doi: 10.1128/JVI.01744-09. Epub 2009 Oct 7.
9
Sequence-divergent chordopoxvirus homologs of the o3 protein maintain functional interactions with components of the vaccinia virus entry-fusion complex.序列差异的痘病毒 o3 蛋白同源物与痘苗病毒进入融合复合物的成分保持功能相互作用。
J Virol. 2012 Feb;86(3):1696-705. doi: 10.1128/JVI.06069-11. Epub 2011 Nov 23.
10
Structural and functional analysis of vaccinia viral fusion complex component protein A28 through NMR and molecular dynamic simulations.通过 NMR 和分子动力学模拟分析牛痘病毒融合复合物成分蛋白 A28 的结构和功能。
PLoS Pathog. 2023 Nov 10;19(11):e1011500. doi: 10.1371/journal.ppat.1011500. eCollection 2023 Nov.

引用本文的文献

1
Antibody Binding and Neutralizing Targets within the Predicted Structure of the Poxvirus Multiprotein Entry-Fusion Complex.痘病毒多蛋白进入融合复合物预测结构中的抗体结合与中和靶点
bioRxiv. 2025 May 7:2025.05.07.652617. doi: 10.1101/2025.05.07.652617.
2
The 2.3 Å Structure of A21, a Protein Component of the Conserved Poxvirus Entry-Fusion Complex.保守痘病毒进入融合复合体的蛋白质组分A21的2.3埃结构
bioRxiv. 2025 Jan 8:2025.01.08.631918. doi: 10.1101/2025.01.08.631918.
3
Poxvirus structural biology for application to vaccine design.

本文引用的文献

1
Cross-Neutralizing and Protective Human Antibody Specificities to Poxvirus Infections.针对痘病毒感染的交叉中和及保护性人类抗体特异性
Cell. 2016 Oct 20;167(3):684-694.e9. doi: 10.1016/j.cell.2016.09.049.
2
Membrane fusion during poxvirus entry.痘病毒进入过程中的膜融合
Semin Cell Dev Biol. 2016 Dec;60:89-96. doi: 10.1016/j.semcdb.2016.07.015. Epub 2016 Jul 14.
3
Dali server update.大理服务器更新。
用于疫苗设计的痘病毒结构生物学
Trends Immunol. 2025 Jun;46(6):455-470. doi: 10.1016/j.it.2025.04.002. Epub 2025 May 7.
4
Which Proteins? The Challenge of Identifying the Protective Antigens for Next-Generation Capripoxvirus Vaccines.哪些蛋白质？鉴定下一代山羊痘病毒疫苗保护性抗原的挑战。
Vaccines (Basel). 2025 Feb 22;13(3):219. doi: 10.3390/vaccines13030219.
5
The 2.3 Å Structure of A21, a Protein Component of the Conserved Poxvirus Entry-Fusion Complex.保守痘病毒进入融合复合体的蛋白质成分A21的2.3埃结构
J Mol Biol. 2025 Jun 15;437(12):169097. doi: 10.1016/j.jmb.2025.169097. Epub 2025 Mar 19.
6
Identification of a Potential Entry-Fusion Complex Based on Sequence Homology of African Swine Fever and Vaccinia Virus.基于非洲猪瘟病毒和牛痘病毒序列同源性鉴定潜在的进入融合复合物。
Viruses. 2024 Feb 23;16(3):349. doi: 10.3390/v16030349.
7
Structural and functional analyses of viral H2 protein of the vaccinia virus entry fusion complex.痘苗病毒进入融合复合体的病毒H2蛋白的结构与功能分析
J Virol. 2023 Dec 21;97(12):e0134323. doi: 10.1128/jvi.01343-23. Epub 2023 Nov 17.
8
Structural and functional analysis of vaccinia viral fusion complex component protein A28 through NMR and molecular dynamic simulations.通过 NMR 和分子动力学模拟分析牛痘病毒融合复合物成分蛋白 A28 的结构和功能。
PLoS Pathog. 2023 Nov 10;19(11):e1011500. doi: 10.1371/journal.ppat.1011500. eCollection 2023 Nov.
9
Exaptation of Inactivated Host Enzymes for Structural Roles in Orthopoxviruses and Novel Folds of Virus Proteins Revealed by Protein Structure Modeling.已失活宿主酶在正痘病毒中结构功能的适应及通过蛋白结构建模揭示病毒蛋白的新折叠。
mBio. 2023 Apr 25;14(2):e0040823. doi: 10.1128/mbio.00408-23. Epub 2023 Apr 5.
10
Widespread Distribution and Evolution of Poxviral Entry-Fusion Complex Proteins in Giant Viruses.痘病毒进入融合复合体蛋白在巨型病毒中的广泛分布与进化
Microbiol Spectr. 2023 Mar 13;11(2):e0494422. doi: 10.1128/spectrum.04944-22.
Nucleic Acids Res. 2016 Jul 8;44(W1):W351-5. doi: 10.1093/nar/gkw357. Epub 2016 Apr 29.
4
Salmon Gill Poxvirus, the Deepest Representative of the Chordopoxvirinae.鲑鱼鳃痘病毒，脊索痘病毒亚科的最具代表性成员。
J Virol. 2015 Sep;89(18):9348-67. doi: 10.1128/JVI.01174-15. Epub 2015 Jul 1.
5
Poxvirus membrane biogenesis.痘病毒膜生物发生
Virology. 2015 May;479-480:619-26. doi: 10.1016/j.virol.2015.02.003. Epub 2015 Feb 26.
6
Ten years of probabilistic estimates of biocrystal solvent content: new insights via nonparametric kernel density estimate.十年生物晶体溶剂含量的概率估计：通过非参数核密度估计获得的新见解。
Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1579-88. doi: 10.1107/S1399004714005550. Epub 2014 May 24.
7
Dendroscope 3: an interactive tool for rooted phylogenetic trees and networks.Dendroscope 3：一个用于有根系统发育树和网络的交互式工具。
Syst Biol. 2012 Dec 1;61(6):1061-7. doi: 10.1093/sysbio/sys062. Epub 2012 Jul 10.
8
The myristate moiety and amino terminus of vaccinia virus l1 constitute a bipartite functional region needed for entry.痘苗病毒 L1 的豆蔻酸部分和氨基末端构成了进入所需的二分功能区域。
J Virol. 2012 May;86(10):5437-51. doi: 10.1128/JVI.06703-11. Epub 2012 Mar 7.
9
The membrane fusion step of vaccinia virus entry is cooperatively mediated by multiple viral proteins and host cell components.痘病毒进入的膜融合步骤是由多种病毒蛋白和宿主细胞成分共同介导的。
PLoS Pathog. 2011 Dec;7(12):e1002446. doi: 10.1371/journal.ppat.1002446. Epub 2011 Dec 15.
10
Interaction between the G3 and L5 proteins of the vaccinia virus entry-fusion complex.痘病毒进入融合复合物中 G3 和 L5 蛋白的相互作用。
Virology. 2011 Apr 10;412(2):278-83. doi: 10.1016/j.virol.2011.01.014. Epub 2011 Feb 4.