A new mutant class, made by targeted mutagenesis, of phage PRD1 reveals that protein P5 connects the receptor binding protein to the vertex.
Phage PRD1 and adenovirus share a number of structural and functional similarities, one of which is the vertex organization at the fivefold-symmetry positions. We developed an in vitro mutagenesis system for the linear PRD1 genome in order to make targeted mutations. The role of protein P5 in the vertex structure was examined by this method. Mutation in gene V revealed that protein P5 is essential. The absence of P5 did not compromise the particle assembly or DNA packaging but led to a deficient vertex structure where the receptor binding protein P2, in addition to protein P5, was missing. P5(-) particles also lost their DNA upon purification. Based on this and previously published information we propose a spatial model for the spike structure at the vertices. This resembles to the corresponding structure in adenovirus.
Department of Biosciences and Institute of Biotechnology, University of Helsinki, 00014 Helsinki, Finland. jaana.bamford@helsinki.fi
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D000327:Adsorption; D002213:Capsid / Q000235:genetics / Q000378:metabolism*; D036022:Capsid Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D008854:Microscopy, Electron; D016297:Mutagenesis, Site-Directed; D011991:Receptors, Virus / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000235:genetics; D017916:Tectiviridae / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly
D036022:Capsid Proteins; D011991:Receptors, Virus; D014764:Viral Proteins; C413083:protein P5, bacteriophage PRD1