Cryo‐EM structure of the Ebola virus nucleoprotein–RNA complex
Ebola virus is an emerging virus that is capable of causing a deadly disease in humans. Replication, transcription and packaging of the viral genome are carried out by the viral nucleocapsid. The nucleocapsid is a complex of the viral nucleoprotein, RNA and several other viral proteins. The nucleopr...
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Published in | Acta crystallographica. Section F, Structural biology communications Vol. 75; no. 5; pp. 340 - 347 |
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Abstract | Ebola virus is an emerging virus that is capable of causing a deadly disease in humans. Replication, transcription and packaging of the viral genome are carried out by the viral nucleocapsid. The nucleocapsid is a complex of the viral nucleoprotein, RNA and several other viral proteins. The nucleoprotein forms large, RNA‐bound, helical filaments and acts as a scaffold for additional viral proteins. The 3.1 Å resolution single‐particle cryo‐electron microscopy structure of the nucleoprotein–RNA helical filament presented here resembles previous structures determined at lower resolution, while providing improved molecular details of protein–protein and protein–RNA interactions. The higher resolution of the structure presented here will facilitate the design and characterization of novel and specific Ebola virus therapeutics targeting the nucleocapsid.
The 3.1 Å resolution single‐particle cryo‐electron microscopy structure of the RNA‐bound Ebola virus nucleoprotein helical filament provides molecular details of protein–protein and protein–RNA interactions. |
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AbstractList | Ebola virus is an emerging virus that is capable of causing a deadly disease in humans. Replication, transcription and packaging of the viral genome are carried out by the viral nucleocapsid. The nucleocapsid is a complex of the viral nucleoprotein, RNA and several other viral proteins. The nucleoprotein forms large, RNA‐bound, helical filaments and acts as a scaffold for additional viral proteins. The 3.1 Å resolution single‐particle cryo‐electron microscopy structure of the nucleoprotein–RNA helical filament presented here resembles previous structures determined at lower resolution, while providing improved molecular details of protein–protein and protein–RNA interactions. The higher resolution of the structure presented here will facilitate the design and characterization of novel and specific Ebola virus therapeutics targeting the nucleocapsid. Ebola virus is an emerging virus that is capable of causing a deadly disease in humans. Replication, transcription and packaging of the viral genome are carried out by the viral nucleocapsid. The nucleocapsid is a complex of the viral nucleoprotein, RNA and several other viral proteins. The nucleoprotein forms large, RNA‐bound, helical filaments and acts as a scaffold for additional viral proteins. The 3.1 Å resolution single‐particle cryo‐electron microscopy structure of the nucleoprotein–RNA helical filament presented here resembles previous structures determined at lower resolution, while providing improved molecular details of protein–protein and protein–RNA interactions. The higher resolution of the structure presented here will facilitate the design and characterization of novel and specific Ebola virus therapeutics targeting the nucleocapsid. The 3.1 Å resolution single‐particle cryo‐electron microscopy structure of the RNA‐bound Ebola virus nucleoprotein helical filament provides molecular details of protein–protein and protein–RNA interactions. The 3.1 Å resolution single-particle cryo-electron microscopy structure of the RNA-bound Ebola virus nucleoprotein helical filament provides molecular details of protein–protein and protein–RNA interactions. Ebola virus is an emerging virus that is capable of causing a deadly disease in humans. Replication, transcription and packaging of the viral genome are carried out by the viral nucleocapsid. The nucleocapsid is a complex of the viral nucleoprotein, RNA and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins. The 3.1 Å resolution single-particle cryo-electron microscopy structure of the nucleoprotein–RNA helical filament presented here resembles previous structures determined at lower resolution, while providing improved molecular details of protein–protein and protein–RNA interactions. The higher resolution of the structure presented here will facilitate the design and characterization of novel and specific Ebola virus therapeutics targeting the nucleocapsid. Ebola virus is an emerging virus that is capable of causing a deadly disease in humans. Replication, transcription and packaging of the viral genome are carried out by the viral nucleocapsid. The nucleocapsid is a complex of the viral nucleoprotein, RNA and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins. The 3.1 Å resolution single-particle cryo-electron microscopy structure of the nucleoprotein-RNA helical filament presented here resembles previous structures determined at lower resolution, while providing improved molecular details of protein-protein and protein-RNA interactions. The higher resolution of the structure presented here will facilitate the design and characterization of novel and specific Ebola virus therapeutics targeting the nucleocapsid.Ebola virus is an emerging virus that is capable of causing a deadly disease in humans. Replication, transcription and packaging of the viral genome are carried out by the viral nucleocapsid. The nucleocapsid is a complex of the viral nucleoprotein, RNA and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins. The 3.1 Å resolution single-particle cryo-electron microscopy structure of the nucleoprotein-RNA helical filament presented here resembles previous structures determined at lower resolution, while providing improved molecular details of protein-protein and protein-RNA interactions. The higher resolution of the structure presented here will facilitate the design and characterization of novel and specific Ebola virus therapeutics targeting the nucleocapsid. |
Author | Kirchdoerfer, Robert N. Ward, Andrew B. Saphire, Erica Ollmann |
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Snippet | Ebola virus is an emerging virus that is capable of causing a deadly disease in humans. Replication, transcription and packaging of the viral genome are... The 3.1 Å resolution single-particle cryo-electron microscopy structure of the RNA-bound Ebola virus nucleoprotein helical filament provides molecular details... |
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SubjectTerms | Amino Acid Sequence Binding Sites Cloning, Molecular Cryoelectron Microscopy cryo‐electron microscopy Ebola virus Ebolavirus Ebolavirus - chemistry Electron microscopy Filaments Gene Expression Genetic Vectors - chemistry Genetic Vectors - metabolism Genomes HEK293 Cells helix Humans Models, Molecular Nucleic Acid Conformation Nucleocapsid - chemistry Nucleocapsid - ultrastructure Nucleocapsids nucleoprotein Nucleoproteins - chemistry Nucleoproteins - genetics Nucleoproteins - metabolism Packaging Protein Binding Protein Conformation, alpha-Helical Protein Interaction Domains and Motifs Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Research Communications Ribonucleic acid RNA RNA viruses RNA, Viral - chemistry RNA, Viral - genetics RNA, Viral - metabolism Sequence Alignment Sequence Homology, Amino Acid Transcription Viral diseases Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - metabolism |
Title | Cryo‐EM structure of the Ebola virus nucleoprotein–RNA complex |
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