Cleavage leads to expansion of bacteriophage P4 procapsids in vitro.
Proteolytic cleavage of the structural proteins is an important part of the maturation process for most bacteriophages and other viruses. In the double-stranded DNA bacteriophages this cleavage is associated with DNA packaging, capsid expansion, and scaffold removal. To understand the role of protein cleavage in the expansion of bacteriophages P2 and P4, we have experimentally cleaved P4 procapsids produced by overexpression of the capsid and scaffolding proteins. The cleavage leads to particle expansion and scaffold removal in vitro. The resulting expanded capsid has a thin-shelled structure similar, but not identical, to that of mature virions.
D000595:Amino Acid Sequence; D017901:Bacteriophage P2 / Q000378:metabolism; D002213:Capsid / Q000378:metabolism* / Q000648:ultrastructure; D036022:Capsid Proteins / Q000737:chemistry / Q000378:metabolism; D020285:Cryoelectron Microscopy; D021621:Imaging, Three-Dimensional; D008969:Molecular Sequence Data; D017900:Myoviridae / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism; D015678:Viral Structural Proteins / Q000378:metabolism; D019065:Virus Assembly
D036022:Capsid Proteins; D015678:Viral Structural Proteins; D014357:Trypsin