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Download Hi-Res ImageDownload to MS-PowerPointCite This:Nano Lett. 2016, 16, 9, 5944-5950
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A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle

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∥ †Department of Bioengineering, ‡Department of Plant and Microbial Biology, §Department of Chemical and Biomolecular Engineering, and ∥Department of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States
# ⊥Berkeley Center for Structural Biology and #Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States
% Department of Chemical and Biological Engineering, Northwestern University, Evanston, Illinois 60091, United States
*E-mail [email protected] (D.T.-E.).
Cite this: Nano Lett. 2016, 16, 9, 5944–5950
Publication Date (Web):August 23, 2016
https://doi.org/10.1021/acs.nanolett.6b02948
Copyright © 2016 American Chemical Society
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    Abstract

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    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.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.nanolett.6b02948.

    • Amino acid abundance of the selected library, additional characterization of VLPs, nucleic acids and Mat protein, electron micrographs of F pilus attachment, crystallographic data, and detailed materials and methods (PDF)

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