Unknown

Dataset Information

0

Multivalent display of proteins on viral nanoparticles using molecular recognition and chemical ligation strategies.


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.

SUBMITTER: Venter PA 

PROVIDER: S-EPMC3114102 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Multivalent display of proteins on viral nanoparticles using molecular recognition and chemical ligation strategies.

Venter P Arno PA   Dirksen Anouk A   Thomas Diane D   Manchester Marianne M   Dawson Philip E PE   Schneemann Anette A  

Biomacromolecules 20110513 6


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 allo  ...[more]

Similar Datasets

| S-EPMC169181 | biostudies-literature
| S-EPMC7284201 | biostudies-literature
| S-EPMC3398510 | biostudies-literature
| S-EPMC8617429 | biostudies-literature
| S-EPMC5518472 | biostudies-literature
| S-EPMC4222322 | biostudies-literature
| S-EPMC2976098 | biostudies-literature
| S-EPMC3580864 | biostudies-literature
| S-EPMC2551747 | biostudies-literature
| S-EPMC8603192 | biostudies-literature