Atomic structure of the Epstein-Barr virus portal
Herpesviridae is a vast family of enveloped DNA viruses that includes eight distinct human pathogens, responsible for diseases that range from almost asymptomatic to severe and life-threatening. Epstein-Barr virus infects B-cells and epithelial cells, causing infectious mononucleosis, as well as a n...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Springer Nature
2019
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| _version_ | 1826296958258511872 |
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| author | Machón, C Fàbrega-Ferrer, M Zhou, D Cuervo, A Carrascosa, J Stuart, D Coll, M |
| author_facet | Machón, C Fàbrega-Ferrer, M Zhou, D Cuervo, A Carrascosa, J Stuart, D Coll, M |
| author_sort | Machón, C |
| collection | OXFORD |
| description | Herpesviridae is a vast family of enveloped DNA viruses that includes eight distinct human pathogens, responsible for diseases that range from almost asymptomatic to severe and life-threatening. Epstein-Barr virus infects B-cells and epithelial cells, causing infectious mononucleosis, as well as a number of cancers. Epstein-Barr infection cannot be cured since neither vaccine nor antiviral drug treatments are available. All herpesviruses contain a linear double-stranded DNA genome, enclosed within an icosahedral capsid. Viral portal protein plays a key role in the procapsid assembly and DNA packaging. The portal is the entrance and exit pore for the viral genome, making it an attractive pharmacological target for the development of new antivirals. Here we present the atomic structure of the portal protein of Epstein-Barr virus, solved by cryo-electron microscopy at 3.5 Å resolution. The detailed architecture of this protein suggests that it plays a functional role in DNA retention during packaging. |
| first_indexed | 2024-03-07T04:24:19Z |
| format | Journal article |
| id | oxford-uuid:cc18b2b5-9ce3-4e2e-ade5-5d785feaac95 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:24:19Z |
| publishDate | 2019 |
| publisher | Springer Nature |
| record_format | dspace |
| spelling | oxford-uuid:cc18b2b5-9ce3-4e2e-ade5-5d785feaac952022-03-27T07:19:27ZAtomic structure of the Epstein-Barr virus portalJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:cc18b2b5-9ce3-4e2e-ade5-5d785feaac95EnglishSymplectic Elements at OxfordSpringer Nature2019Machón, CFàbrega-Ferrer, MZhou, DCuervo, ACarrascosa, JStuart, DColl, MHerpesviridae is a vast family of enveloped DNA viruses that includes eight distinct human pathogens, responsible for diseases that range from almost asymptomatic to severe and life-threatening. Epstein-Barr virus infects B-cells and epithelial cells, causing infectious mononucleosis, as well as a number of cancers. Epstein-Barr infection cannot be cured since neither vaccine nor antiviral drug treatments are available. All herpesviruses contain a linear double-stranded DNA genome, enclosed within an icosahedral capsid. Viral portal protein plays a key role in the procapsid assembly and DNA packaging. The portal is the entrance and exit pore for the viral genome, making it an attractive pharmacological target for the development of new antivirals. Here we present the atomic structure of the portal protein of Epstein-Barr virus, solved by cryo-electron microscopy at 3.5 Å resolution. The detailed architecture of this protein suggests that it plays a functional role in DNA retention during packaging. |
| spellingShingle | Machón, C Fàbrega-Ferrer, M Zhou, D Cuervo, A Carrascosa, J Stuart, D Coll, M Atomic structure of the Epstein-Barr virus portal |
| title | Atomic structure of the Epstein-Barr virus portal |
| title_full | Atomic structure of the Epstein-Barr virus portal |
| title_fullStr | Atomic structure of the Epstein-Barr virus portal |
| title_full_unstemmed | Atomic structure of the Epstein-Barr virus portal |
| title_short | Atomic structure of the Epstein-Barr virus portal |
| title_sort | atomic structure of the epstein barr virus portal |
| work_keys_str_mv | AT machonc atomicstructureoftheepsteinbarrvirusportal AT fabregaferrerm atomicstructureoftheepsteinbarrvirusportal AT zhoud atomicstructureoftheepsteinbarrvirusportal AT cuervoa atomicstructureoftheepsteinbarrvirusportal AT carrascosaj atomicstructureoftheepsteinbarrvirusportal AT stuartd atomicstructureoftheepsteinbarrvirusportal AT collm atomicstructureoftheepsteinbarrvirusportal |