title: Controlled encapsulation of multiple proteins in virus capsids.
abstract: Multiple proteins can be bound within the Cowpea Chlorotic Mottle Virus capsid shell in an efficient and controlled manner by using heterodimeric coiled-coil peptide oligomers. Through genetic modification, these oligomers can be attached to the capsid protein and an enhanced green fluorescent protein (EGFP). In this way, the capsid proteins can be noncovalently bound to EGFP prior to the induction of the capsid assembly. Up to 15 EGFP proteins can be encapsulated per capsid in a controlled and efficient manner.
authors.affiliation: Institute for Molecules and Materials, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
authors.forename: Inge J
authors.initials: IJ
authors.lastname: Minten
authors.forename: Linda J A
authors.initials: LJ
authors.lastname: Hendriks
authors.forename: Roeland J M
authors.initials: RJ
authors.lastname: Nolte
authors.forename: Jeroen J L M
authors.initials: JJ
authors.lastname: Cornelissen
mesh_terms: D017795:Bromovirus / Q000737:chemistry*; D002213:Capsid / Q000737:chemistry*; D036022:Capsid Proteins / Q000737:chemistry*; D049452:Green Fluorescent Proteins / Q000032:analysis* / Q000737:chemistry*
chemical_list: D036022:Capsid Proteins; C485184:enhanced green fluorescent protein; D049452:Green Fluorescent Proteins