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Structure. 2011 Jul 13;19(7):1011-20. doi: 10.1016/j.str.2011.03.023.

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

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1
The Division of Structural Biology and the Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK.

Abstract

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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PMID:
21742267
PMCID:
PMC3136756
DOI:
10.1016/j.str.2011.03.023
[Indexed for MEDLINE]
Free PMC Article

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