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