Thermostable exoshells fold and stabilize recombinant proteins.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 29129910.
- Also identified by DOI 10.1038/s41467-017-01585-2 and PMC identifier 5682286.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The expression and stabilization of recombinant proteins is fundamental to basic and applied biology. Here we have engineered a thermostable protein nanoparticle (tES) to improve both expression and stabilization of recombinant proteins using this technology. tES provides steric accommodation and charge complementation to green fluorescent protein (GFPuv), horseradish peroxidase (HRPc), and Renilla luciferase (rLuc), improving the yields of functional in vitro folding by ~100-fold. Encapsulated enzymes retain the ability to metabolize small-molecule substrates, presumably via four 4.5-nm pores present in the tES shell. GFPuv exhibits no spectral shifts in fluorescence compared to a nonencapsulated control. Thermolabile proteins internalized by tES are resistant to thermal, organic, chaotropic, and proteolytic denaturation and can be released from the tES assembly with mild pH titration followed by proteolysis.
Medical subject headings
- Archaeoglobus fulgidus
- Escherichia coli
- Green Fluorescent Proteins
- Horseradish Peroxidase
- Luciferases, Renilla
- Recombinant Proteins