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Secretion of biologically-active human interferon-β by Bacillus subtilis
Hiroshi Kakeshita1, Yasushi Kageyama, Keiji Endo
1Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba, Ibaraki 305-8572, Japan. hkakeshi@sakura.cc.tsukuba.ac.jp
Biotechnology Letters
|May 6, 2011
Summary
The Bacillus subtilis AmyE propeptide significantly boosts human interferon-beta secretion by over four-fold. Co-expressing PrsA further enhances this effect, showing additive benefits for protein production.
Area of Science:
- Microbiology
- Protein Engineering
- Biotechnology
Background:
- Heterologous protein secretion in Bacillus subtilis is crucial for industrial applications.
- Enhancing secretion efficiency of proteins like human interferon-beta (hIFN-β) remains a challenge.
Purpose of the Study:
- To investigate the impact of the Bacillus subtilis AmyE propeptide on hIFN-β secretion.
- To evaluate the synergistic effect of AmyE propeptide and PrsA co-expression on hIFN-β production.
Main Methods:
- Utilized human interferon-beta (hIFN-β) as a model heterologous protein.
- Assessed secretion levels and biological activity of hIFN-β with and without AmyE propeptide.
- Examined the influence of co-expressing PrsA alongside AmyE propeptide.
Main Results:
- AmyE propeptide increased hIFN-β secretion and activity by over four-fold.
- Co-expression of PrsA with AmyE propeptide resulted in an additional 1.5-fold increase in secretion and activity.
- Demonstrated an additive enhancement effect of AmyE propeptide and PrsA on hIFN-β production.
Conclusions:
- The Bacillus subtilis AmyE propeptide is a potent enhancer for heterologous protein secretion.
- Co-expression of PrsA provides an additive benefit, further improving secretion yields.
- These findings offer a strategy to optimize the production of therapeutic proteins in B. subtilis.
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