Cryo-EM structure of the Ebola virus nucleoprotein–RNA complex at 3.6 Å resolution

• Published in: Nature (London) Vol. 563; no. 7729; pp. 137 - 140
• Main Authors: Sugita, Yukihiko, Matsunami, Hideyuki, Kawaoka, Yoshihiro, Noda, Takeshi, Wolf, Matthias
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.11.2018; Nature Publishing Group
• Subjects: 101/28; 631/326/596/2042; 631/535/1258/1259; 82/80; 82/83; Antiviral agents; Assembly; Atoms; Cells (Biology); Cryoelectron Microscopy; Drug development; Ebola virus; Ebolavirus; Ebolavirus - chemistry; Ebolavirus - ultrastructure; Electron microscopy; Electrostatic properties; Filoviridae; Genetic aspects; Genomes; Genomics; HEK293 Cells; Hemorrhagic fever; Hemorrhagic fevers; Humanities and Social Sciences; Humans; Hydrophobicity; Letter; Mammalian cells; Measles; Microscopy; Models, Molecular; multidisciplinary; Nucleocapsid - chemistry; Nucleocapsid - ultrastructure; Nucleocapsids; Nucleoproteins; Nucleotide sequence; Oligomerization; Oligomers; Organic chemistry; Primates; Protein binding; Ribonucleic acid; RNA; RNA viruses; RNA, Viral - chemistry; RNA, Viral - ultrastructure; Science; Structure; Tomography; Transcription (Genetics); Virions; Virus replication; Viruses; Visualization; VP24 protein; Family Filoviridae; Helium Accumulation; Near-atomic Resolution; Ebola Virus; Single-particle Cryo-electron Microscopy

Ebola virus causes haemorrhagic fever with a high fatality rate in humans and non-human primates. It belongs to the family Filoviridae in the order Mononegavirales , which are viruses that contain linear, non-segmented, negative-sense, single-stranded genomic RNA 1 , 2 . The enveloped, filamentous v...