Mechanism of assembly of recombinant murine polyomavirus-like particles.
VP1 is the major viral coat protein of murine polyomavirus and can be used for the generation of virus-like particles in vitro. Here, we demonstrate that capsid assembly is an equilibrium reaction followed by oxidation of intracapsomere disulfide bonds, which are not essential for the formation of virus-like particles but enable complete particle assembly and prevent capsid disassembly.
Schmidt
U
U
Institut f]ur Biotechnologie, Martin-Luther-Universit]at Halle-Wittenberg, D-06120 Halle (Saale), Germany. uli.schmidt@biochemtech.uni-halle.de
Rudolph
R
R
Böhm
G
G
D000818:Animals; D002213:Capsid; D036022:Capsid Proteins; D004220:Disulfides; D004926:Escherichia coli; D015870:Gene Expression; D051379:Mice; D011120:Polyomavirus / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics; D011995:Recombination, Genetic; D014771:Virion / Q000502:physiology; D019065:Virus Assembly / Q000502:physiology
D036022:Capsid Proteins; D004220:Disulfides; D011993:Recombinant Fusion Proteins; C062481:VP1 protein, polyomavirus