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Biomacromolecules. 2013 Sep 9;14(9):2989-95. doi: 10.1021/bm400796c. Epub 2013 Aug 27.

Location of the bacteriophage P22 coat protein C-terminus provides opportunities for the design of capsid-based materials.

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1
Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, United States.

Abstract

Rational design of modifications to the interior and exterior surfaces of virus-like particles (VLPs) for future therapeutic and materials applications is based on structural information about the capsid. Existing cryo-electron microscopy-based models suggest that the C-terminus of the bacteriophage P22 coat protein (CP) extends toward the capsid exterior. Our biochemical analysis through genetic manipulations of the C-terminus supports the model where the CP C-terminus is exposed on the exterior of the P22 capsid. Capsids displaying a 6xHis tag appended to the CP C-terminus bind to a Ni affinity column, and the addition of positively or negatively charged coiled coil peptides to the capsid results in association of these capsids upon mixing. Additionally, a single cysteine appended to the CP C-terminus results in the formation of intercapsid disulfide bonds and can serve as a site for chemical modifications. Thus, the C-terminus is a powerful location for multivalent display of peptides that facilitate nanoscale assembly and capsid modification.

PMID:
23957641
PMCID:
PMC3882140
DOI:
10.1021/bm400796c
[Indexed for MEDLINE]
Free PMC Article
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