The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture.
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.
Merckel
Michael C
MC
Programme on Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, P.O. Box 65, Viikinkaari 1 00014, Finland.
Huiskonen
Juha T
JT
Bamford
Dennis H
DH
Goldman
Adrian
A
Tuma
Roman
R
D000260:Adenoviruses, Human / Q000737:chemistry; D000595:Amino Acid Sequence; D025622:Bacteriophage PRD1 / Q000737:chemistry*; D002213:Capsid / Q000737:chemistry*; D036022:Capsid Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D019143:Evolution, Molecular; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013059:Spectrum Analysis, Raman; D014409:Tumor Necrosis Factor-alpha / Q000737:chemistry; D014764:Viral Proteins / Q000737:chemistry*
D036022:Capsid Proteins; D014409:Tumor Necrosis Factor-alpha; D014764:Viral Proteins