Controlled encapsulation of multiple proteins in virus capsids

Inge J. Minten, Linda J.A. Hendriks, Roeland J.M. Nolte, Jeroen Johannes Lambertus Maria Cornelissen

Research output: Contribution to journalArticleAcademicpeer-review

145 Citations (Scopus)

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
Original languageUndefined
Pages (from-to)17771-17773
Number of pages3
JournalJournal of the American Chemical Society
Volume131
Issue number49
DOIs
Publication statusPublished - 2009

Keywords

  • IR-77783
  • METIS-263228

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