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Orthogonal labeling of M13 minor capsid proteins with DNA to self-assemble end-to-end multiphage structures.


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.

SUBMITTER: Hess GT 

PROVIDER: S-EPMC3905569 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

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Orthogonal labeling of M13 minor capsid proteins with DNA to self-assemble end-to-end multiphage structures.

Hess Gaelen T GT   Guimaraes Carla P CP   Spooner Eric E   Ploegh Hidde L HL   Belcher Angela M AM  

ACS synthetic biology 20130528 9


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  ...[more]

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