Orthogonal Labeling of M13 Minor Capsid Proteins with DNA to Self-Assemble End-to-End Multiphage Structures
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Ploegh_Orthogonal labeling.pdf
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Author(s)
Hess, Gaelen T.
Guimaraes, Carla P.
Spooner, Eric
Ploegh, Hidde
Belcher, Angela M
Date Issued
September 2013
Journal
ACS Synthetic Biology
Publisher
American Chemical Society (ACS)
Citation
Hess, Gaelen T., Carla P. Guimaraes, Eric Spooner, Hidde L. Ploegh, and Angela M. Belcher. “Orthogonal Labeling of M13 Minor Capsid Proteins with DNA to Self-Assemble End-to-End Multiphage Structures.” ACS Synthetic Biology 2, no. 9 (September 20, 2013): 490–496. © 2013 American Chemical Society.
Version
Final published version
Abstract
M13 bacteriophage has been used as a scaffold to organize materials for various applications. Building more complex multiphage devices requires precise control of interactions between the M13 capsid proteins. Toward this end, we engineered a loop structure onto the pIII capsid protein of M13 bacteriophage to enable sortase-mediated labeling reactions for C-terminal display. Combining this with N-terminal sortase-mediated labeling, we thus created a phage scaffold that can be labeled orthogonally on three capsid proteins: the body and both ends. We show that covalent attachment of different DNA oligonucleotides at the ends of the new phage structure enables formation of multiphage particles oriented in a specific order. These have potential as nanoscale scaffolds for multi-material devices.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Materials Science and Engineering
Koch Institute for Integrative Cancer Research at MIT
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1021/sb400019s
