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A new potential secretion pathway for recombinant proteins in Bacillus subtilis
Guangqiang Wang1,2, Yongjun Xia3, Zhennan Gu4,5
1School of Medical Instrument and Food Engineering, University of Shanghai for Science and Technology, Shanghai, 200093, People's Republic of China. 1015wanggq@163.com.
Microbial Cell Factories
|November 12, 2015
Summary
This study explores using non-classical protein secretion pathways in Bacillus subtilis to improve recombinant protein export. Researchers found that non-classical secreted proteins can effectively signal the export of various model proteins into the culture medium.
Area of Science:
- Microbiology
- Biotechnology
- Molecular Biology
Background:
- Secreting cytoplasmic proteins into growth media offers advantages for biotechnology.
- Bacillus subtilis is a promising host for recombinant protein production due to its lack of an outer membrane.
- Classical secretion pathways in B. subtilis face bottlenecks, limiting large-scale recombinant protein secretion.
Purpose of the Study:
- To investigate the potential of non-classical protein secretion pathways for enhanced recombinant protein export.
- To determine if non-classically secreted proteins can act as signals for exporting model recombinant proteins.
Main Methods:
- Utilized four distinct non-classically secreted proteins as signal peptides.
- Tested the ability of these signals to export three model recombinant proteins: nucleoskeletal-like protein (Nsp), alkaline phosphatase (PhoA), and β-galactosidase (BgaB).
Main Results:
- All four non-classical signals successfully directed the export of the intrinsically disordered Nsp.
- Two non-classical signals facilitated the secretion of PhoA.
- One non-classical signal enabled the secretion of thermostable BgaB, a protein not secreted via standard Sec-dependent signals.
Conclusions:
- Non-classically secreted proteins can effectively mediate the export of recombinant proteins to the culture medium.
- Non-classical protein secretion pathways represent a novel and viable strategy for improving recombinant protein production in Bacillus subtilis.
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