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观察沙粒病毒核蛋白七聚体组装。

Observation of arenavirus nucleoprotein heptamer assembly.

机构信息

Laboratoire Architecture et Fonction des Macromolécules Biologiques (AFMB), Aix-Marseille University and CNRS, France.

School of Life & Health Sciences, Aston University, Birmingham, UK.

出版信息

FEBS Open Bio. 2021 Apr;11(4):1076-1083. doi: 10.1002/2211-5463.13106. Epub 2021 Feb 25.

Abstract

Arenaviruses are enveloped viruses containing a segmented, negative, and ambisense single-stranded RNA genome wrapped with a nucleoprotein (NP). The NP is the most abundant viral protein in infected cells and plays a critical role in both replication/transcription and virion assembly. The NP associates with RNA to form a ribonucleoprotein (RNP) complex, and this implies self-assembly while the exact structure of this polymer is not yet known. Here, we report a measurement of the full-length Mopeia virus NP by negative stain transmission electron microscopy. We observed RNP complex particles with diameter 15 ± 1 nm as well as symmetric circular heptamers of the same diameter, consistent with previous observations.

摘要

沙粒病毒为有包膜的病毒,含有分段、负义、单链、反义的 RNA 基因组,被核蛋白(NP)所包裹。NP 是感染细胞中含量最丰富的病毒蛋白,在复制/转录和病毒颗粒组装中均发挥关键作用。NP 与 RNA 结合形成核糖核蛋白(RNP)复合物,提示存在自我组装,但其聚合物的确切结构尚不清楚。本研究通过负染透射电子显微镜报告了全长 Mopeia 病毒 NP 的测量结果。我们观察到直径为 15±1nm 的 RNP 复合物颗粒以及相同直径的对称圆形七聚体,与先前的观察结果一致。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3dab/8016135/5560237f5c37/FEB4-11-1076-g004.jpg

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