Implementation of p22 viral capsids as nanoplatforms.
Viral capsids are dynamic macromolecular machines which self-assemble and undergo concerted conformational changes during their life cycle. We have taken advantage of the inherent structural flexibility of viral capsids and generated two morphologically different types of viral nanoplatforms from the bacteriophage P22 capsids. Their interior surfaces were genetically manipulated for site-specific attachment of a biotin linker. The extent of internal modifications in each capsid form was characterized by high-resolution mass spectrometry and the analyses revealed that the reactivity of the genetically introduced residues located on the internal surface changes according to the structural transformation of the capsid. Internally modified capsids having 10 nm diameter pores at the 12 icosahedral vertices, so-called wiffle-balls (WB), exhibited the capability to entrap the large tetrameric protein complex streptavidin via the biotin linker anchored onto the interior surface of the WB.
Kang
Sebyung
S
Department of Chemistry and Biochemistry and Center for Bio-Inspired Nanomaterials, Montana State University, Bozeman, MT 59717, USA.
Uchida
Masaki
M
O'Neil
Alison
A
Li
Rui
R
Prevelige
Peter E
PE
Douglas
Trevor
T
D017100:Bacteriophage P22 / Q000737:chemistry* / Q000235:genetics; D001710:Biotin / Q000737:chemistry; D002213:Capsid / Q000737:chemistry*; D002850:Chromatography, Gel; D003432:Cross-Linking Reagents / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D008301:Maleimides / Q000737:chemistry; D008958:Models, Molecular; D009154:Mutation; D049329:Nanostructures / Q000737:chemistry*; D015202:Protein Engineering / Q000379:methods; D021241:Spectrometry, Mass, Electrospray Ionization; D019809:Streptavidin / Q000737:chemistry; D013499:Surface Properties; D014162:Transfection
D003432:Cross-Linking Reagents; D008301:Maleimides; C043592:maleimide; D001710:Biotin; D019809:Streptavidin