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Published on: September 10, 2021
Streptomyces protein secretion and its application in biotechnology
Mohamed Belal Hamed1,2, Jozef Anné1, Spyridoula Karamanou1
1KU Leuven, Rega Institute for Medical Research, Department of Microbiology and Immunology, Laboratory of Molecular Bacteriology, 3000 Leuven, Belgium.
Gram-positive bacteria efficiently secrete proteins, avoiding inclusion bodies. This review discusses optimizing recombinant protein production using bacterial secretion pathways, particularly in Streptomyces lividans.
Area of Science:
- Microbiology
- Biotechnology
- Biochemistry
Background:
- Gram-positive bacteria are crucial for industrial production of metabolites and proteins.
- They secrete proteins directly into the medium, simplifying downstream processing and avoiding inclusion bodies.
- Recombinant protein production in these hosts can be limited by secretion efficiency, protein folding, degradation, and metabolic load.
Purpose of the Study:
- To review protein secretion pathways in Gram-positive bacteria.
- To discuss strategies for optimizing recombinant protein yield.
- To present optimization approaches using the Streptomyces lividans model.
Main Methods:
- Review of existing literature on bacterial protein secretion pathways.
- Analysis of challenges in recombinant protein production.
- Discussion of optimization strategies for Streptomyces lividans.
Main Results:
- Eight protein secretion pathways exist in Gram-positive bacteria, with the general secretion (Sec) and Twin-arginine (Tat) pathways being most relevant for recombinant production.
- Challenges include inefficient secretion, misfolding, proteolysis, and host metabolic burden.
- Optimization strategies can enhance protein secretion and overall yield.
Conclusions:
- Streptomyces lividans is a valuable model for studying and optimizing heterologous protein secretion.
- The discussed approaches are broadly applicable to other Gram-positive bacterial hosts.
- Improving secretion efficiency is key to maximizing recombinant protein production.
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