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Quantitative Measurement of Intrathecally Synthesized Proteins in Mice

Quantitative Measurement of Intrathecally Synthesized Proteins in Mice

Published on: November 29, 2019

Human G-CSF synthesis using stress-responsive bacterial proteins.

Jong-Am Song¹, Kyung-Yeon Han, Jin-Seung Park

¹Department of Chemical and Biological Engineering, Korea University, Seoul, South Korea.

FEMS Microbiology Letters

|May 23, 2009

Summary

Bacterial stress proteins enhance the solubility and native conformation of aggregation-prone proteins like human granulocyte colony-stimulating factor (hG-CSF) when used as fusion partners in Escherichia coli.

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Area of Science:

Biotechnology
Molecular Biology
Protein Expression

Background:

Heterologous protein expression in E. coli often leads to aggregation into inclusion bodies.
Stress-responsive proteins in Escherichia coli are upregulated under specific stress conditions.

Purpose of the Study:

To investigate the potential of bacterial stress-responsive proteins as fusion partners for improving the solubility of aggregation-prone proteins.
To assess the conformational integrity of expressed proteins when fused with stress-responsive partners.

Main Methods:

Exposure of Escherichia coli BL21(DE3) to 2-hydroxyethyl disulfide to induce stress.
Fusion expression of human granulocyte colony-stimulating factor (hG-CSF) with identified stress-responsive proteins (PpiB, Bfr, YjdC, FolA, CheZ, GshB).
Analysis of hG-CSF solubility and confirmation of native conformation using circular dichroism spectroscopy.

Main Results:

Several stress-responsive proteins were significantly upregulated in E. coli under oxidative stress.
Fusion of hG-CSF with these stress proteins dramatically enhanced its solubility in the E. coli cytoplasm.
Purified hG-CSF, when fused, exhibited identical circular dichroism spectra to standard hG-CSF, indicating native conformation.

Conclusions:

Bacterial stress-responsive proteins are effective fusion partners for enhancing the solubility of aggregation-prone heterologous proteins in E. coli.
This strategy facilitates the production of correctly folded recombinant proteins in the cytoplasm.
The use of stress-responsive fusion partners offers a promising approach for recombinant protein production in microbial systems.