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马尔堡病毒单层核衣壳蛋白-RNA 复合物的冷冻电镜结构。

Cryo-EM structure of single-layered nucleoprotein-RNA complex from Marburg virus.

机构信息

Max Planck Institute of Biochemistry, Research Group Molecular Structural Biology, Martinsried, Germany.

iHuman Institute, ShanghaiTech University, Shanghai, China.

出版信息

Nat Commun. 2024 Nov 27;15(1):10307. doi: 10.1038/s41467-024-54431-7.

DOI:10.1038/s41467-024-54431-7
PMID:39604358
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11603049/
Abstract

Marburg virus (MARV) causes lethal hemorrhagic fever in humans, posing a threat to global health. We determined by cryogenic electron microscopy (cryo-EM) the MARV helical ribonucleoprotein (RNP) complex structure in single-layered conformation, which differs from the previously reported structure of a double-layered helix. Our findings illuminate novel RNP interactions and expand knowledge on MARV genome packaging and nucleocapsid assembly, both processes representing attractive targets for the development of antiviral therapeutics against MARV disease.

摘要

马尔堡病毒 (MARV) 可导致人类致命性出血热，对全球健康构成威胁。我们通过低温电子显微镜 (cryo-EM) 确定了 MARV 螺旋核糖核蛋白 (RNP) 复合物的单层构象结构，这与之前报道的双层螺旋结构不同。我们的发现阐明了新的 RNP 相互作用，并扩展了 MARV 基因组包装和核衣壳组装的知识，这两个过程都是针对 MARV 疾病开发抗病毒治疗的有吸引力的靶标。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75c1/11603049/186eaaf0fae9/41467_2024_54431_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75c1/11603049/6d9f33b5165a/41467_2024_54431_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75c1/11603049/53b4f090292b/41467_2024_54431_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75c1/11603049/52f9d763ef89/41467_2024_54431_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75c1/11603049/186eaaf0fae9/41467_2024_54431_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75c1/11603049/6d9f33b5165a/41467_2024_54431_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75c1/11603049/53b4f090292b/41467_2024_54431_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75c1/11603049/52f9d763ef89/41467_2024_54431_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75c1/11603049/186eaaf0fae9/41467_2024_54431_Fig4_HTML.jpg

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J Infect Dis. 2023 Jul 14;228(2):103-105. doi: 10.1093/infdis/jiad161.
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PNAS Nexus. 2023 Apr 6;2(4):pgad120. doi: 10.1093/pnasnexus/pgad120. eCollection 2023 Apr.
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Nucleic Acids Res. 2023 Jan 6;51(D1):D678-D689. doi: 10.1093/nar/gkac1003.
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Ebola and Marburg virus VP35 coiled-coil validated as antiviral target by tripartite split-GFP complementation.通过三方分裂绿色荧光蛋白互补验证埃博拉病毒和马尔堡病毒VP35卷曲螺旋结构作为抗病毒靶点
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