A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle

Michael A. Asensio, Norma M. Morella, Christopher M. Jakobson, Emily C. Hartman, Jeff E. Glasgow, Banumathi Sankaran, Peter H. Zwart, Danielle Tullman-Ercek*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Virus-like particles are used to encapsulate drugs, imaging agents, enzymes, and other biologically active molecules in order to enhance their function. However, the size of most virus-like particles is inflexible, precluding the design of appropriately sized containers for different applications. Here, we describe a chromatographic selection for virus-like particle assembly. Using this selection, we identified a single amino acid substitution to the coat protein of bacteriophage MS2 that mediates a uniform switch in particle geometry from T = 3 to T = 1 icosahedral symmetry. The resulting smaller particle retains the ability to be disassembled and reassembled in vitro and to be chemically modified to load cargo into its interior cavity. The pair of 27 and 17 nm MS2 particles will allow direct examination of the effect of size on function in established applications of virus-like particles, including drug delivery and imaging.

Original languageEnglish (US)
Pages (from-to)5944-5950
Number of pages7
JournalNano letters
Volume16
Issue number9
DOIs
StatePublished - Sep 14 2016

Keywords

  • Protein engineering
  • bacteriophage MS2
  • drug delivery
  • nanocontainers
  • protein supramolecular structure
  • virus structure

ASJC Scopus subject areas

  • Bioengineering
  • Chemistry(all)
  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanical Engineering

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