1. Multivalent display of proteins on viral nanoparticles using molecular recognition and chemical ligation strategies
- Author
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Philip E. Dawson, Diane Thomas, Marianne Manchester, Anouk Dirksen, Anette Schneemann, and P. Arno Venter
- Subjects
Polymers and Plastics ,Bacterial Toxins ,Blotting, Western ,Supramolecular chemistry ,Heterologous ,Bioengineering ,Spodoptera ,Transfection ,Maltose-Binding Proteins ,Article ,Biomaterials ,Maltose-binding protein ,Mice ,Molecular recognition ,Antigen ,Oximes ,Materials Chemistry ,Escherichia coli ,Animals ,Nanotechnology ,Cloning, Molecular ,Antigens, Bacterial ,Mice, Inbred BALB C ,Aniline Compounds ,biology ,Virion ,Stereoisomerism ,Surface Plasmon Resonance ,Recombinant Proteins ,Cell biology ,Nanostructures ,Microscopy, Electron ,Biochemistry ,biology.protein ,Target protein ,Chemical ligation ,Baculoviridae ,Plasmids - Abstract
Multivalent display of heterologous proteins on viral nanoparticles forms a basis for numerous applications in nanotechnology, including vaccine development, targeted therapeutic delivery, and tissue-specific bioimaging. In many instances, precise placement of proteins is required for optimal functioning of the supramolecular assemblies, but orientation- and site-specific coupling of proteins to viral scaffolds remains a significant technical challenge. We have developed two strategies that allow for controlled attachment of a variety of proteins on viral particles using covalent and noncovalent principles. In one strategy, an interaction between domain 4 of anthrax protective antigen and its receptor was used to display multiple copies of a target protein on virus-like particles. In the other, expressed protein ligation and aniline-catalyzed oximation was used to display covalently a model protein. The latter strategy, in particular, yielded nanoparticles that induced potent immune responses to the coupled protein, suggesting potential applications in vaccine development.
- Published
- 2011