Tale of two spikes in bacteriophage PRD1.
Structural comparisons between bacteriophage PRD1 and adenovirus have revealed an evolutionary relationship that has contributed significantly to current ideas on virus phylogeny. However, the structural organization of the receptor-binding spike complex and how the different symmetry mismatches are mediated between the spike-complex proteins are not clear. We determined the architecture of the PRD1 spike complex by using electron microscopy and three-dimensional image reconstruction of a series of PRD1 mutants. We constructed an atomic model for the full-length P5 spike protein by using comparative modeling. P5 was shown to be bound directly to the penton base protein P31. P5 and the receptor-binding protein P2 form two separate spikes, interacting with each other near the capsid shell. P5, with a tumor necrosis factor-like head domain, may have been responsible for host recognition before capture of the current receptor-binding protein P2.
Huiskonen
Juha T
JT
Department of Biological and Environmental Sciences, Institute of Biotechnology, P.O. Box 65 (Viikinkaani 1), University of Helsinki, FI-0014, Helsinki, Finland.
Manole
Violeta
V
Butcher
Sarah J
SJ
D025622:Bacteriophage PRD1 / Q000737:chemistry* / Q000648:ultrastructure; D036022:Capsid Proteins / Q000737:chemistry* / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D006026:Glycoside Hydrolases; D008958:Models, Molecular; D017376:Viral Tail Proteins / Q000737:chemistry* / Q000648:ultrastructure
D036022:Capsid Proteins; D017376:Viral Tail Proteins; C413083:protein P5, bacteriophage PRD1; D006026:Glycoside Hydrolases; C083268:tailspike protein, bacteriophage