title: Mechanism of assembly of recombinant murine polyomavirus-like particles.
abstract: 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.
authors.affiliation: Institut f]ur Biotechnologie, Martin-Luther-Universit]at Halle-Wittenberg, D-06120 Halle (Saale), Germany. uli.schmidt@biochemtech.uni-halle.de
authors.forename: U
authors.initials: U
authors.lastname: Schmidt
authors.forename: R
authors.initials: R
authors.lastname: Rudolph
authors.forename: G
authors.initials: G
authors.lastname: Böhm
mesh_terms: 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
chemical_list: D036022:Capsid Proteins; D004220:Disulfides; D011993:Recombinant Fusion Proteins; C062481:VP1 protein, polyomavirus