Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.

The morphogenesis of poxviruses such as vaccinia virus (VACV) sees the virion shape mature from spherical to brick-shaped. Trimeric capsomers of the VACV D13 protein form a transitory, stabilizing lattice on the surface of the initial spherical immature virus particle. The crystal structure of D13 r...

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Main Authors: Bahar, M, Graham, S, Stuart, D, Grimes, J
Format: Journal article
Language:English
Published: 2011
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author Bahar, M
Graham, S
Stuart, D
Grimes, J
author_facet Bahar, M
Graham, S
Stuart, D
Grimes, J
author_sort Bahar, M
collection OXFORD
description The morphogenesis of poxviruses such as vaccinia virus (VACV) sees the virion shape mature from spherical to brick-shaped. Trimeric capsomers of the VACV D13 protein form a transitory, stabilizing lattice on the surface of the initial spherical immature virus particle. The crystal structure of D13 reveals that this major scaffolding protein comprises a double β barrel "jelly-roll" subunit arranged as pseudo-hexagonal trimers. These structural features are characteristic of the major capsid proteins of a lineage of large icosahedral double-stranded DNA viruses including human adenovirus and the bacteriophages PRD1 and PM2. Structure-based phylogenetic analysis confirms that VACV belongs to this lineage, suggesting that (analogously to higher organism embryogenesis) early poxvirus morphogenesis reflects their evolution from a lineage of viruses sharing a common icosahedral ancestor.
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spelling oxford-uuid:aaece297-bfaa-4086-a052-b30944b88ecb2022-03-27T03:18:25ZInsights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:aaece297-bfaa-4086-a052-b30944b88ecbEnglishSymplectic Elements at Oxford2011Bahar, MGraham, SStuart, DGrimes, JThe morphogenesis of poxviruses such as vaccinia virus (VACV) sees the virion shape mature from spherical to brick-shaped. Trimeric capsomers of the VACV D13 protein form a transitory, stabilizing lattice on the surface of the initial spherical immature virus particle. The crystal structure of D13 reveals that this major scaffolding protein comprises a double β barrel "jelly-roll" subunit arranged as pseudo-hexagonal trimers. These structural features are characteristic of the major capsid proteins of a lineage of large icosahedral double-stranded DNA viruses including human adenovirus and the bacteriophages PRD1 and PM2. Structure-based phylogenetic analysis confirms that VACV belongs to this lineage, suggesting that (analogously to higher organism embryogenesis) early poxvirus morphogenesis reflects their evolution from a lineage of viruses sharing a common icosahedral ancestor.
spellingShingle Bahar, M
Graham, S
Stuart, D
Grimes, J
Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.
title Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.
title_full Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.
title_fullStr Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.
title_full_unstemmed Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.
title_short Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.
title_sort insights into the evolution of a complex virus from the crystal structure of vaccinia virus d13
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AT grimesj insightsintotheevolutionofacomplexvirusfromthecrystalstructureofvacciniavirusd13