The unique vertex of bacterial virus PRD1 is connected to the viral internal membrane.
Icosahedral double-stranded DNA (dsDNA) bacterial viruses are known to package their genomes into preformed procapsids via a unique portal vertex. Bacteriophage PRD1 differs from the more commonly known icosahedral dsDNA phages in that it contains an internal lipid membrane. The packaging of PRD1 is known to proceed via preformed empty capsids. Now, a unique vertex has been shown to exist in PRD1. We show in this study that this unique vertex extends to the virus internal membrane via two integral membrane proteins, P20 and P22. These small membrane proteins are necessary for the binding of the putative packaging ATPase P9, via another capsid protein, P6, to the virus particle.
Department of Biosciences and Institute of Biotechnology, Biocenter 2, FIN-00014 University of Helsinki, Finland.
Nelli J
NJ
Strömsten
Dennis H
DH
Bamford
Jaana K H
JK
Bamford
D025622:Bacteriophage PRD1 / Q000235:genetics / Q000378:metabolism; D002213:Capsid / Q000378:metabolism*; D002460:Cell Line; D004926:Escherichia coli / Q000821:virology; D007425:Intracellular Membranes / Q000378:metabolism*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D019779:Salmonella enterica / Q000821:virology; D015678:Viral Structural Proteins / Q000235:genetics / Q000378:metabolism; D014771:Virion / Q000378:metabolism / Q000648:ultrastructure; D019065:Virus Assembly
D008565:Membrane Proteins; D015678:Viral Structural Proteins