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Production of Recombinant PRMT Proteins using the Baculovirus Expression Vector System

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Recombinant protein production using the Semliki Forest Virus expression system.

H D Blasey¹, K Lundström, S Tate

¹Glaxo Institute for Molecular Biology, 14 Chemin des Aulx, CH 1228, Plan les Ouates, Switzerland.

|February 24, 2012

Summary

This study scaled up transient recombinant protein expression to litre scale using the Semliki Forest Virus system. Optimal conditions were found for producing substantial amounts of human cyclooxygenase-2.

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High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension

High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension

Published on: December 28, 2015

Area of Science:

Biotechnology
Molecular Biology
Virology

Background:

Transient gene expression systems are crucial for producing recombinant proteins.
Scaling up these systems presents challenges in maintaining efficiency and yield.
Semliki Forest Virus (SFV) is a powerful tool for high-level transient protein expression.

Purpose of the Study:

To optimize and scale up transient recombinant protein expression using the Semliki Forest Virus (SFV) system to the litre scale.
To identify optimal conditions for SFV-mediated protein expression in mammalian cells.
To demonstrate the successful production of a specific microsomal enzyme, human cyclooxygenase-2, at litre scale.

Main Methods:

Comparative analysis of bacterial β-galactosidase expression in BHK and CHO cells.
Optimization of infection parameters including medium composition (10% FCS, pH 6.9), infection volume, and multiplicity of infection (MOI).
Application of optimized conditions for litre-scale suspension culture production of human cyclooxygenase-2 using SFV in BHK cells.

Main Results:

Optimal conditions for BHK cell infection identified: 10% FCS, pH 6.9, small infection volumes, and high MOI.
Stirring was found to not impact the infection process.
Successful litre-scale production yielded substantial and reproducible amounts of human cyclooxygenase-2 (16 mg microsomal protein/10^9 cells) with high specific activity (3942 ± 765 pg PGE2/μg microsomal protein/5 min).

Conclusions:

The Semliki Forest Virus (SFV) system is effective for scalable transient recombinant protein production.
Optimized conditions enable reproducible, high-yield expression of complex proteins like human cyclooxygenase-2 at litre scale.
This methodology provides a robust platform for producing valuable recombinant proteins for research and potential therapeutic applications.