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Nat Cell Biol. 2019 Apr;21(4):452-461. doi: 10.1038/s41556-019-0300-y. Epub 2019 Apr 1.
2
Single-Molecule Imaging and Computational Microscopy Approaches Clarify the Mechanism of the Dimerization and Membrane Interactions of Green Fluorescent Protein.单分子成像和计算显微镜方法阐明了绿色荧光蛋白二聚化和膜相互作用的机制。
Int J Mol Sci. 2019 Mar 20;20(6):1410. doi: 10.3390/ijms20061410.
3
The role of exosomal transport of viral agents in persistent HIV pathogenesis.病毒因子外泌体转运在持续性 HIV 发病机制中的作用。
Retrovirology. 2018 Dec 22;15(1):79. doi: 10.1186/s12977-018-0462-x.
4
A stochastic assembly model for Nipah virus revealed by super-resolution microscopy.超级分辨率显微镜揭示的尼帕病毒随机组装模型。
Nat Commun. 2018 Aug 3;9(1):3050. doi: 10.1038/s41467-018-05480-2.
5
Shedding light on the cell biology of extracellular vesicles.揭示细胞外囊泡的细胞生物学。
Nat Rev Mol Cell Biol. 2018 Apr;19(4):213-228. doi: 10.1038/nrm.2017.125. Epub 2018 Jan 17.
6
Palmitoylation Contributes to Membrane Curvature in Influenza A Virus Assembly and Hemagglutinin-Mediated Membrane Fusion.棕榈酰化作用在甲型流感病毒组装及血凝素介导的膜融合过程中对膜曲率有贡献。
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Multiple Strategies Reveal a Bidentate Interaction between the Nipah Virus Attachment and Fusion Glycoproteins.多种策略揭示了尼帕病毒附着糖蛋白与融合糖蛋白之间的双齿相互作用。
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9
Nipah virus matrix protein: expert hacker of cellular machines.尼帕病毒基质蛋白:细胞机器的专业“黑客”
FEBS Lett. 2016 Aug;590(15):2494-511. doi: 10.1002/1873-3468.12272. Epub 2016 Jul 12.
10
Nipah Virus C Protein Recruits Tsg101 to Promote the Efficient Release of Virus in an ESCRT-Dependent Pathway.尼帕病毒C蛋白招募Tsg101以通过依赖内体分选转运复合体(ESCRT)的途径促进病毒的有效释放。
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超级分辨率显微镜揭示的尼帕病毒基质蛋白的纳米级组织。

The nanoscale organization of Nipah virus matrix protein revealed by super-resolution microscopy.

机构信息

Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada; Life Sciences Institute, University of British Columbia, Vancouver, British Columbia, Canada.

Institute of Parasitology, McGill University, Sainte-Anne-de-Bellevue, Québec, Canada.

出版信息

Biophys J. 2022 Jun 21;121(12):2290-2296. doi: 10.1016/j.bpj.2022.05.026. Epub 2022 May 25.

DOI:10.1016/j.bpj.2022.05.026
PMID:35614854
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9279348/
Abstract

The matrix proteins (M) of many enveloped RNA viruses mediate virus assembly and budding. However, it remains poorly understood how M are involved in virus budding and how they interact with envelope proteins. Here, we show that the expression level of Nipah (NiV) M in particles produced by the host cells deviates from a gamma distribution and does not reflect that of the host cells, indicating assembly of the NiV-M in the process. Our data reveal that NiV-M affects the circularity of the particles while the NiV envelope proteins do not. The organization of NiV envelope proteins on the membrane of the particles is similar to those that do not express NiV-M, suggesting that NiV-M does not directly interact with the envelope proteins during assembly and budding.

摘要

许多包膜 RNA 病毒的基质蛋白(M)介导病毒的组装和出芽。然而,M 如何参与病毒出芽以及它们如何与包膜蛋白相互作用仍知之甚少。在这里,我们表明,宿主细胞产生的颗粒中的尼帕病毒(NiV)M 的表达水平偏离了伽马分布,并且不反映宿主细胞的表达水平,表明 NiV-M 在该过程中进行组装。我们的数据表明 NiV-M 影响颗粒的圆度,而 NiV 包膜蛋白则不影响。颗粒膜上 NiV 包膜蛋白的组织类似于不表达 NiV-M 的那些,表明 NiV-M 在组装和出芽过程中不与包膜蛋白直接相互作用。