Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus.
Semliki Forest virus serves as a paradigm for membrane fusion and assembly. Our icosahedral reconstruction combined 5276 particle images from 48 cryo-electron micrographs and determined the virion structure to 9 A resolution. The improved resolution of this map reveals an N-terminal arm linking caps...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2000
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| _version_ | 1797083141380243456 |
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| author | Mancini, E Clarke, M Gowen, B Rutten, T Fuller, S |
| author_facet | Mancini, E Clarke, M Gowen, B Rutten, T Fuller, S |
| author_sort | Mancini, E |
| collection | OXFORD |
| description | Semliki Forest virus serves as a paradigm for membrane fusion and assembly. Our icosahedral reconstruction combined 5276 particle images from 48 cryo-electron micrographs and determined the virion structure to 9 A resolution. The improved resolution of this map reveals an N-terminal arm linking capsid subunits and defines the spike-capsid interaction sites. It illustrates the paired helical nature of the transmembrane segments and the elongated structures connecting them to the spike projecting domains. A 10 A diameter density in the fusion protein lines the cavity at the center of the spike. These clearly visible features combine with the variation in order between the layers to provide a framework for understanding the structural changes during the life cycle of an enveloped virus. |
| first_indexed | 2024-03-07T01:37:39Z |
| format | Journal article |
| id | oxford-uuid:95c01df8-96b6-4eb0-8c63-1a6bbac20c26 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:37:39Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:95c01df8-96b6-4eb0-8c63-1a6bbac20c262022-03-26T23:48:20ZCryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:95c01df8-96b6-4eb0-8c63-1a6bbac20c26EnglishSymplectic Elements at Oxford2000Mancini, EClarke, MGowen, BRutten, TFuller, SSemliki Forest virus serves as a paradigm for membrane fusion and assembly. Our icosahedral reconstruction combined 5276 particle images from 48 cryo-electron micrographs and determined the virion structure to 9 A resolution. The improved resolution of this map reveals an N-terminal arm linking capsid subunits and defines the spike-capsid interaction sites. It illustrates the paired helical nature of the transmembrane segments and the elongated structures connecting them to the spike projecting domains. A 10 A diameter density in the fusion protein lines the cavity at the center of the spike. These clearly visible features combine with the variation in order between the layers to provide a framework for understanding the structural changes during the life cycle of an enveloped virus. |
| spellingShingle | Mancini, E Clarke, M Gowen, B Rutten, T Fuller, S Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. |
| title | Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. |
| title_full | Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. |
| title_fullStr | Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. |
| title_full_unstemmed | Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. |
| title_short | Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. |
| title_sort | cryo electron microscopy reveals the functional organization of an enveloped virus semliki forest virus |
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