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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 beta 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.
Insights into the evolution of a complex virus from the crystal structure of vaccinia virus d13.,Bahar MW, Graham SC, Stuart DI, Grimes JM Structure. 2011 Jul 13;19(7):1011-20. PMID:21742267[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Bahar MW, Graham SC, Stuart DI, Grimes JM. Insights into the evolution of a complex virus from the crystal structure of vaccinia virus d13. Structure. 2011 Jul 13;19(7):1011-20. PMID:21742267 doi:10.1016/j.str.2011.03.023
