Orthogonal Labeling of M13 Minor Capsid Proteins with DNA to Self-Assemble End-to-End Multiphage Structures

• Main Authors: Hess, Gaelen T. (Contributor), Guimaraes, Carla P. (Author), Spooner, Eric (Author), Ploegh, Hidde (Contributor), Belcher, Angela M (Author)
• Other Authors: Massachusetts Institute of Technology. Department of Biological Engineering (Contributor), Massachusetts Institute of Technology. Department of Biology (Contributor), Massachusetts Institute of Technology. Department of Materials Science and Engineering (Contributor), Koch Institute for Integrative Cancer Research at MIT (Contributor), Belcher, Angela M. (Contributor)
• Format: Article
• Language: English
• Published: American Chemical Society (ACS), 2014-11-20T17:55:46Z.
• Subjects: Article
• Online Access: Get fulltext

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.
United States. Army Research Office (Institute for Collaborative Biotechnologies, grant W911NF-09-0001)