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Multivalent Display Using Hybrid Virus Nanoparticles

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Book cover Protein Scaffolds

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1798))

Abstract

Many important biological interactions are multivalent and often sensitive to spatial organization. Nonenveloped viruses are a natural source of scaffolds for building multivalent ligands to probe these types of interactions which avoid complex synthetic schemes required for other types of scaffolds. The coat protein (CP) of bacteriophage Qβ can be fused to protein domains and coexpressed with the unfused CP to produce hybrid nanoparticles with high exterior loading of xenogenic protein domains. These hybrid nanoparticles are simple to produce in large quantity. Starting from cDNAs for the virus CP and a codon-optimized ligand domain of interest, bulk purification can be completed in as little as 3 weeks. Major phases of the work involve the cloning of cDNAs into plasmid vectors, test expressions for hybrid nanoparticle formation, and purification by selective precipitation and ultracentrifugation. For uncomplicated protein domains, laboratory culture yields as high as 50 mg/L and 30 protein domains per particle have been routinely achieved.

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Author information

Authors and Affiliations

  1. Department of Gastroenterology, University of California—San Diego, La Jolla, CA, USA

    Steven D. Brown

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  1. Steven D. Brown
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Editor information

Editors and Affiliations

  1. Department of Chemistry, Occidental College, Los Angeles, California, USA

    Andrew K. Udit

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Brown, S.D. (2018). Multivalent Display Using Hybrid Virus Nanoparticles. In: Udit, A. (eds) Protein Scaffolds. Methods in Molecular Biology, vol 1798. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7893-9_10

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  • DOI: https://doi.org/10.1007/978-1-4939-7893-9_10

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-7892-2

  • Online ISBN: 978-1-4939-7893-9

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