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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.

Original publication

DOI

10.1016/j.str.2011.03.023

Type

Journal article

Journal

Structure

Publication Date

13/07/2011

Volume

19

Pages

1011 - 1020

Keywords

Amino Acid Sequence, Bacteriophage PRD1, Biological Evolution, Capsid, Capsid Proteins, Cloning, Molecular, Corticoviridae, Crystallization, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Phylogeny, Plasmids, Protein Conformation, Protein Structure, Secondary, Recombinant Fusion Proteins, Transfection, Vaccinia, Vaccinia virus