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Published on: December 28, 2015
Intein-mediated high-yield expression of recombinant teriparatide
Ruocheng Gu1, Rouyu Di2, Chunle Yang3
1Department of Microbial Physiological & Metabolic Engineering, State Key Laboratory of Microbial Diversity and Innovative Utilization, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
This study introduces a novel intein-mediated expression system using a gp41-1 mutant to improve the production of teriparatide (rPTH) for osteoporosis treatment. The new method significantly enhances yield and purity, paving the way for efficient industrial manufacturing.
Area of Science:
- Biotechnology
- Protein Engineering
- Pharmacology
Background:
- Teriparatide (recombinant parathyroid hormone) is crucial for osteoporosis treatment.
- Current biosynthesis faces challenges: host degradation, low yield, and costly tag removal.
Purpose of the Study:
- To develop a high-yield, cost-effective expression system for teriparatide.
- To address limitations of current recombinant protein production methods.
Main Methods:
- Fusion of teriparatide with a gp41-1 mutant intein for traceless cleavage.
- Optimization of fed-batch fermentation with refined induction and carbon source strategies.
- Development of a secondary purification protocol.
Main Results:
- The D107Ggp41-1 intein showed low in vivo cleavage (30-40%) and high in vitro efficiency (90% in 4h).
- Optimized fermentation achieved a final teriparatide yield of 1.3 g/L.
- Recombinant teriparatide (rTeriparatide) purity exceeded 98% after purification.
Conclusions:
- The developed gp41-1-mediated expression system enables scalable, high-yield teriparatide production.
- This system offers a promising foundation for the efficient industrial manufacturing of teriparatide.
- The study overcomes key challenges in recombinant protein biosynthesis.
