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Transient Expression and Cellular Localization of Recombinant Proteins in Cultured Insect Cells
Published on: April 20, 2017
Chaperone and foldase coexpression in the baculovirus-insect cell expression system.
M J Betenbaugh1, E Ailor, E Whiteley
1Department of Chemical Engineering, The Johns Hopkins University, 21218-2694, Baltimore, Maryland, U.S.A..
Cytotechnology
|February 24, 2012
Summary
The baculovirus-insect cell expression system (BEVS) is widely used for recombinant protein production. Optimizing folding and secretion pathways by coexpressing chaperones and foldases can enhance yields of complex proteins.
Area of Science:
- Biotechnology
- Molecular Biology
- Protein Expression
Background:
- The baculovirus-insect cell expression system (BEVS) is a key platform for producing recombinant proteins.
- Challenges in BEVS include protein aggregation and inefficient processing, particularly for secreted and membrane proteins.
Purpose of the Study:
- To explore strategies for enhancing recombinant protein production in BEVS.
- To investigate the role of coexpressed chaperones and foldases in improving protein folding, assembly, and secretion.
Main Methods:
- Engineering the folding, assembly, and secretion pathways within the BEVS.
- Coexpression of chaperones and foldases with the target recombinant protein.
Main Results:
- Coexpression of chaperones and foldases can create an optimal environment for protein folding and assembly.
- This approach has the potential to increase yields of valuable complex proteins.
Conclusions:
- Engineering BEVS pathways by coexpressing chaperones and foldases is a promising strategy to overcome production limitations.
- Future work may involve optimizing oligosaccharide modification and secretion factors for improved protein secretion and glycosylation.
- BEVS serves as a valuable in vivo eukaryotic system for studying protein folding and secretion mechanisms.
