• 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

M1 羧基端结构域的两个极性残基对于流感 A 病毒粒子的形成至关重要。

Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.

机构信息

Center for Molecular Virology, CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.

Department of Biophysics, Health Science Center, Peking University, Beijing, 100191, China.

出版信息

Cell Microbiol. 2015 Nov;17(11):1583-93. doi: 10.1111/cmi.12457. Epub 2015 May 29.

DOI:10.1111/cmi.12457
PMID:25939747
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4682459/
Abstract

The matrix protein 1 (M1) is the most abundant structural protein in influenza A virus particles. It oligomerizes to form the matrix layer under the lipid membrane, sustaining stabilization of the morphology of the virion. The present study indicates that M1 forms oligomers based on a fourfold symmetrical oligomerization pattern. Further analysis revealed that the oligomerization pattern of M1 was controlled by a highly conserved region within the C-terminal domain. Two polar residues of this region, serine-183 (S183) and threonine-185 (T185), were identified to be critical for the oligomerization pattern of M1. M1 point mutants suggest that single S183A or T185A substitution could result in the production of morphologically filamentous particles, while double substitutions, M1-S183A/T185A, totally disrupted the fourfold symmetry and resulted in the failure of virus production. These data indicate that the polar groups in these residues are essential to control the oligomerization pattern of M1. Thus, the present study will aid in determining the mechanisms of influenza A virus matrix layer formation during virus morphogenesis.

摘要

基质蛋白 1（M1）是甲型流感病毒粒子中含量最丰富的结构蛋白。它寡聚化形成脂质膜下的基质层，维持病毒形态的稳定性。本研究表明，M1 基于四元对称寡聚化模式形成寡聚体。进一步分析表明，M1 的寡聚化模式受 C 末端结构域内高度保守区域的控制。该区域的两个极性残基丝氨酸-183（S183）和苏氨酸-185（T185）被鉴定为 M1 寡聚化模式的关键。M1 点突变体表明，单个 S183A 或 T185A 取代可能导致形态丝状颗粒的产生，而双取代 M1-S183A/T185A 则完全破坏了四元对称并导致病毒产生失败。这些数据表明，这些残基中的极性基团对于控制 M1 的寡聚化模式至关重要。因此，本研究将有助于确定流感病毒基质层在病毒形态发生过程中的形成机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/0c4d70fe1c03/cmi0017-1583-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/f9ea1cf97ae9/cmi0017-1583-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/ae5539a9f93e/cmi0017-1583-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/1d02216d5b7e/cmi0017-1583-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/7b895cec6b9a/cmi0017-1583-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/0c4d70fe1c03/cmi0017-1583-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/f9ea1cf97ae9/cmi0017-1583-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/ae5539a9f93e/cmi0017-1583-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/1d02216d5b7e/cmi0017-1583-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/7b895cec6b9a/cmi0017-1583-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf91/4682459/0c4d70fe1c03/cmi0017-1583-f5.jpg

相似文献

1
Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.M1 羧基端结构域的两个极性残基对于流感 A 病毒粒子的形成至关重要。
Cell Microbiol. 2015 Nov;17(11):1583-93. doi: 10.1111/cmi.12457. Epub 2015 May 29.
2
Involvement of an Arginine Triplet in M1 Matrix Protein Interaction with Membranes and in M1 Recruitment into Virus-Like Particles of the Influenza A(H1N1)pdm09 Virus.精氨酸三联体在甲型H1N1pdm09流感病毒M1基质蛋白与膜的相互作用以及M1募集到病毒样颗粒中的作用
PLoS One. 2016 Nov 4;11(11):e0165421. doi: 10.1371/journal.pone.0165421. eCollection 2016.
3
Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions.鉴定甲型流感病毒M1基质蛋白中与核蛋白（NP）结合、寡聚化及掺入病毒粒子所需的结构域。
J Gen Virol. 2007 Aug;88(Pt 8):2280-2290. doi: 10.1099/vir.0.82809-0.
4
Deep Mutational Scan of the Highly Conserved Influenza A Virus M1 Matrix Protein Reveals Substantial Intrinsic Mutational Tolerance.深度突变扫描高度保守的流感病毒 M1 基质蛋白揭示了大量内在突变容忍性。
J Virol. 2019 Jun 14;93(13). doi: 10.1128/JVI.00161-19. Print 2019 Jul 1.
5
Reverse genetics studies on the filamentous morphology of influenza A virus.甲型流感病毒丝状形态的反向遗传学研究
J Gen Virol. 2003 Mar;84(Pt 3):517-527. doi: 10.1099/vir.0.18803-0.
6
Mutations in the Influenza A Virus M1 Protein Enhance Virus Budding To Complement Lethal Mutations in the M2 Cytoplasmic Tail.甲型流感病毒M1蛋白的突变增强病毒出芽，以补偿M2细胞质尾中的致死突变。
J Virol. 2017 Dec 14;92(1). doi: 10.1128/JVI.00858-17. Print 2018 Jan 1.
7
Amphipathic alpha-helices and putative cholesterol binding domains of the influenza virus matrix M1 protein are crucial for virion structure organisation.流感病毒基质蛋白 M1 中的两亲性α-螺旋和推定的胆固醇结合结构域对于病毒粒子结构的组织至关重要。
Virus Res. 2015 Dec 2;210:114-8. doi: 10.1016/j.virusres.2015.07.017. Epub 2015 Jul 23.
8
Phosphatidylserine Lateral Organization Influences the Interaction of Influenza Virus Matrix Protein 1 with Lipid Membranes.磷脂酰丝氨酸的侧向组织影响流感病毒基质蛋白1与脂质膜的相互作用。
J Virol. 2017 May 26;91(12). doi: 10.1128/JVI.00267-17. Print 2017 Jun 15.
9
Basic residues of the helix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motifs.参与M1核转运的流感病毒M1蛋白六螺旋结构域的碱性残基可被PTAP和YPDL晚期组装结构域基序取代。
J Virol. 2003 Jun;77(12):7078-92. doi: 10.1128/jvi.77.12.7078-7092.2003.
10
The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation.甲型流感病毒的M1和M2蛋白是丝状颗粒形成的重要决定因素。
Virology. 1998 Jan 5;240(1):127-37. doi: 10.1006/viro.1997.8916.

引用本文的文献

1
Inhibitory effects of a hot-water extract of cumin fruit on influenza A virus infection.孜然果实热水提取物对甲型流感病毒感染的抑制作用。
PLoS One. 2025 Jun 27;20(6):e0326423. doi: 10.1371/journal.pone.0326423. eCollection 2025.
2
Region-selective and site-specific glycation of influenza proteins surrounding the viral envelope membrane.流感病毒包膜周围蛋白质的区域选择性和位点特异性糖基化。
Sci Rep. 2024 Aug 16;14(1):18975. doi: 10.1038/s41598-024-69793-7.
3
Adaptation potential of H3N8 canine influenza virus in human respiratory cells.

本文引用的文献

1
Structural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH.甲型流感病毒基质蛋白M1及其在低pH值下的自组装结构分析
PLoS One. 2013 Dec 16;8(12):e82431. doi: 10.1371/journal.pone.0082431. eCollection 2013.
2
The genetics of virus particle shape in equine influenza A virus.马流感病毒粒子形态的遗传学研究。
Influenza Other Respir Viruses. 2013 Dec;7 Suppl 4(Suppl 4):81-9. doi: 10.1111/irv.12197.
3
Specific residues in the 2009 H1N1 swine-origin influenza matrix protein influence virion morphology and efficiency of viral spread in vitro.
H3N8 犬流感病毒在人呼吸道细胞中的适应潜力。
Sci Rep. 2024 Aug 13;14(1):18750. doi: 10.1038/s41598-024-69509-x.
4
Structural dynamics of SARS-CoV-2 nucleocapsid protein induced by RNA binding.RNA 结合诱导的 SARS-CoV-2 核衣壳蛋白的结构动力学
PLoS Comput Biol. 2022 May 12;18(5):e1010121. doi: 10.1371/journal.pcbi.1010121. eCollection 2022 May.
5
Conformational triggers associated with influenza matrix protein 1 polymerization.与流感基质蛋白 1 聚合相关的构象触发。
J Biol Chem. 2021 Jan-Jun;296:100316. doi: 10.1016/j.jbc.2021.100316. Epub 2021 Jan 29.
6
The native structure of the assembled matrix protein 1 of influenza A virus.甲型流感病毒聚合基质蛋白 1 的天然结构。
Nature. 2020 Nov;587(7834):495-498. doi: 10.1038/s41586-020-2696-8. Epub 2020 Sep 9.
7
Genetic Analysis of the M Gene of Equine Influenza Virus Strains Isolated in Poland, in the Context of the Asian-like Group Formation.在亚洲样毒株形成的背景下，对波兰分离的马流感病毒株M基因的遗传分析
J Vet Res. 2018 Dec 31;62(4):405-412. doi: 10.2478/jvetres-2018-0057. eCollection 2018 Dec.
8
Conserved methionine 165 of matrix protein contributes to the nuclear import and is essential for influenza A virus replication.基质蛋白中保守的蛋氨酸 165 有助于核输入，对于甲型流感病毒的复制是必需的。
Virol J. 2018 Dec 3;15(1):187. doi: 10.1186/s12985-018-1056-x.
9
Maintaining pH-dependent conformational flexibility of M1 is critical for efficient influenza A virus replication.维持 M1 依赖 pH 的构象灵活性对于流感 A 病毒的有效复制至关重要。
Emerg Microbes Infect. 2017 Dec 6;6(12):e108. doi: 10.1038/emi.2017.96.
10
Mutations in the Influenza A Virus M1 Protein Enhance Virus Budding To Complement Lethal Mutations in the M2 Cytoplasmic Tail.甲型流感病毒M1蛋白的突变增强病毒出芽，以补偿M2细胞质尾中的致死突变。
J Virol. 2017 Dec 14;92(1). doi: 10.1128/JVI.00858-17. Print 2018 Jan 1.
2009 年 H1N1 猪源流感病毒基质蛋白中的特定残基影响病毒粒子的形态和体外病毒传播的效率。
PLoS One. 2012;7(11):e50595. doi: 10.1371/journal.pone.0050595. Epub 2012 Nov 27.
4
Structure and assembly of a paramyxovirus matrix protein.副黏病毒基质蛋白的结构与组装。
Proc Natl Acad Sci U S A. 2012 Aug 28;109(35):13996-4000. doi: 10.1073/pnas.1210275109. Epub 2012 Aug 13.
5
Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domain.甲型流感病毒 M1 蛋白的结构解析：N 端结构域的 pH 依赖性寡聚化和 C 端结构域的二聚化。
PLoS One. 2012;7(5):e37786. doi: 10.1371/journal.pone.0037786. Epub 2012 May 24.
6
Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions.电子冷冻断层摄影术显示麻疹病毒的基质蛋白如何在完整病毒粒子内部包裹核糖核蛋白。
Proc Natl Acad Sci U S A. 2011 Nov 1;108(44):18085-90. doi: 10.1073/pnas.1105770108. Epub 2011 Oct 24.
7
Spatial structure peculiarities of influenza A virus matrix M1 protein in an acidic solution that simulates the internal lysosomal medium.流感 A 病毒基质 M1 蛋白在模拟内部溶酶体介质的酸性溶液中的空间结构特征。
FEBS J. 2011 Dec;278(24):4905-16. doi: 10.1111/j.1742-4658.2011.08392.x. Epub 2011 Oct 31.
8
[Disordered regions in C-domain structure of influenza virus M1 protein].[流感病毒M1蛋白C结构域中的无序区域]
Mol Biol (Mosk). 2011 Jul-Aug;45(4):689-96.
9
The SUMOylation of matrix protein M1 modulates the assembly and morphogenesis of influenza A virus.基质蛋白 M1 的 SUMOylation 调节甲型流感病毒的组装和形态发生。
J Virol. 2011 Jul;85(13):6618-28. doi: 10.1128/JVI.02401-10. Epub 2011 Apr 20.
10
Vaccine potential of Nipah virus-like particles.尼帕病毒样颗粒的疫苗潜力。
PLoS One. 2011 Apr 6;6(4):e18437. doi: 10.1371/journal.pone.0018437.