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Publication Abstract from PubMed

Comparisons of bacteriophage PRD1 and adenovirus protein structures and virion architectures have been instrumental in unraveling an evolutionary relationship and have led to a proposal of a phylogeny-based virus classification. The structure of the PRD1 spike protein P5 provides further insight into the evolution of viral proteins. The crystallized P5 fragment comprises two structural domains: a globular knob and a fibrous shaft. The head folds into a ten-stranded jelly roll beta barrel, which is structurally related to the tumor necrosis factor (TNF) and the PRD1 coat protein domains. The shaft domain is a structural counterpart to the adenovirus spike shaft. The structural relationships between PRD1, TNF, and adenovirus proteins suggest that the vertex proteins may have originated from an ancestral TNF-like jelly roll coat protein via a combination of gene duplication and deletion.

The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture.,Merckel MC, Huiskonen JT, Bamford DH, Goldman A, Tuma R Mol Cell. 2005 Apr 15;18(2):161-70. PMID:15837420^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.