Encapsulation of Exogenous Proteins in Vault Nanoparticles

Meng Wang; Danny Abad; Valerie A Kickhoefer; Leonard H Rome; Shaily Mahendra

doi:10.1007/978-1-4939-7893-9_3

Encapsulation of Exogenous Proteins in Vault Nanoparticles

Methods Mol Biol. 2018:1798:25-37. doi: 10.1007/978-1-4939-7893-9_3.

Authors

Meng Wang¹, Danny Abad², Valerie A Kickhoefer², Leonard H Rome², Shaily Mahendra³

Affiliations

¹ Department of Civil and Environmental Engineering, University of California, Los Angeles, CA, USA.
² Department of Biological Chemistry, University of California, Los Angeles, CA, USA.
³ Department of Civil and Environmental Engineering, University of California, Los Angeles, CA, USA. mahendra@seas.ucla.edu.

PMID: 29868949
DOI: 10.1007/978-1-4939-7893-9_3

Abstract

Natural vault nanoparticles are ribonucleoprotein particles with a mass of 13 MDa that have been found in a wide variety of eukaryotes. Empty recombinant vaults are assembled from heterologously expressed Major Vault Protein (MVP), forming the barrel-shaped vault shell. These structures are morphologically indistinguishable from natural vault particles. Here, we describe the packaging and purification of exogenous proteins into these recombinant vault particles by mixing with proteins attached to the INT domain that binds to MVP.

Keywords: Baculovirus expression; Enzyme immobilization; Nanocages; Nanostructures; Protein scaffold.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Animals
Enzymes, Immobilized
Gene Expression
Genetic Vectors / genetics
Genetic Vectors / metabolism
Nanoparticles* / chemistry
Nanoparticles* / ultrastructure
Nanotechnology
Rats
Recombinant Fusion Proteins / chemistry
Sf9 Cells
Vault Ribonucleoprotein Particles* / chemistry

Substances

Enzymes, Immobilized
Recombinant Fusion Proteins
Vault Ribonucleoprotein Particles
major vault protein