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Structure and assembly of the Ebola virus nucleocapsid
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Structure and assembly of the Ebola virus nucleocapsid
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Journal Article
Structure and assembly of the Ebola virus nucleocapsid
2017
Overview
Application of cryo-electron tomography and subtomogram averaging to determine the structure of the Ebola virus nucleocapsid within intact viruses and recombinant nucleocapsid-like assemblies.
Assembling Ebola's box
The Ebola virus nucleocapsid—a protein shell—encloses, or 'encapsidates', the viral genome and acts as a scaffold for virus assembly and as a template for genome replication. John Briggs and colleagues use cryo-electron tomography to solve the structure of the nucleocapsid of the Ebola virus. They use the structures of the Ebola virus nucleocapsid within intact viruses and recombinant assemblies to propose a model for viral RNA encapsidation and accessory protein recruitment.
Ebola and Marburg viruses are filoviruses: filamentous, enveloped viruses that cause haemorrhagic fever
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. Filoviruses are within the order Mononegavirales
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, which also includes rabies virus, measles virus, and respiratory syncytial virus. Mononegaviruses have non-segmented, single-stranded negative-sense RNA genomes that are encapsidated by nucleoprotein and other viral proteins to form a helical nucleocapsid. The nucleocapsid acts as a scaffold for virus assembly and as a template for genome transcription and replication. Insights into nucleoprotein–nucleoprotein interactions have been derived from structural studies of oligomerized, RNA-encapsidating nucleoprotein
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,
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,
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,
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, and cryo-electron microscopy of nucleocapsid
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,
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,
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,
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,
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,
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or nucleocapsid-like structures
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,
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,
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. There have been no high-resolution reconstructions of complete mononegavirus nucleocapsids. Here we apply cryo-electron tomography and subtomogram averaging to determine the structure of Ebola virus nucleocapsid within intact viruses and recombinant nucleocapsid-like assemblies. These structures reveal the identity and arrangement of the nucleocapsid components, and suggest that the formation of an extended α-helix from the disordered carboxy-terminal region of nucleoprotein-core links nucleoprotein oligomerization, nucleocapsid condensation, RNA encapsidation, and accessory protein recruitment.
Publisher
Nature Publishing Group UK,Nature Publishing Group
