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.