Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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