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Encapsulation of Exogenous Proteins in Vault Nanoparticles
Meng Wang1, Danny Abad2, Valerie A Kickhoefer2
1Department of Civil and Environmental Engineering, University of California, Los Angeles, CA, USA.
Methods in Molecular Biology (Clifton, N.J.)
|June 6, 2018
Summary
Recombinant vault nanoparticles, assembled from Major Vault Protein (MVP), can package exogenous proteins. This method uses INT-tagged proteins for efficient binding and purification of these large ribonucleoprotein particles.
Area of Science:
- Biochemistry
- Molecular Biology
- Nanotechnology
Background:
- Vault nanoparticles are large (13 MDa) ribonucleoprotein particles found in eukaryotes.
- Recombinant vaults can be assembled in vitro from the Major Vault Protein (MVP).
- These recombinant structures mimic natural vaults morphologically.
Purpose of the Study:
- To describe a method for packaging exogenous proteins into recombinant vault nanoparticles.
- To demonstrate the purification of these protein-loaded vault particles.
Main Methods:
- Assembly of empty recombinant vaults from heterologously expressed MVP.
- Attachment of exogenous proteins to an INT domain that binds MVP.
- Mixing of INT-tagged proteins with vault shells for packaging.
- Purification of the resulting protein-loaded vault particles.
Main Results:
- Successful packaging of exogenous proteins into recombinant vault particles was achieved.
- The packaging process utilizes the specific binding interaction between the INT domain and MVP.
- Purification yielded morphologically intact, protein-loaded vault structures.
Conclusions:
- Recombinant vault nanoparticles provide a viable system for the encapsulation of exogenous proteins.
- This technique offers a novel approach for protein delivery and purification using vault structures.
- The method is scalable and adaptable for various protein payloads.
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