Journal
FUTURE MICROBIOLOGY
Volume 8, Issue 2, Pages 191-208Publisher
FUTURE MEDICINE LTD
DOI: 10.2217/FMB.12.133
Keywords
gene copy number; peroxisome; promoter; protein folding; protein secretion; proteomics; transcriptomics; transformation
Categories
Funding
- Austrian Science Fund (FWF)
- Austrian Research Promotion Agency
- European Science Foundation (ESF)
- Federal Ministry of Economy, Family and Youth (BMWFJ)
- Federal Ministry of Transport, Innovation and Technology (bmvit)
- Styrian Business Promotion Agency (SFG)
- Standortagentur Tirol
- ZIT - Technology Agency of the City of Vienna through the COMET-Funding Program
- doctoral program 'BioToP - Biomolecular Technology of Proteins' (Austrian Science Fund, FWF) [W1224]
- Polymun Scientific GmbH
- Biomin Research Center, Boehringer-Ingelheim RCV
- Biocrates Life Sciences AG
- Lonza AG
- VTU Technology GmbH
- Sandoz GmbH
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Pichia pastoris is the most frequently used yeast system for heterologous protein production today. The last few years have seen several products based on this platform reach approval as biopharmaceutical drugs. Successful glycoengineering to humanize N-glycans is further fuelling this development. However, detailed understanding of the yeast's physiology, genetics and regulation has only developed rapidly in the last few years since published genome sequences have become available. An expanding toolbox of genetic elements and strains for the improvement of protein production is being generated, including promoters, gene copy-number enhancement, gene knockout and high-throughput methods. Protein folding and secretion have been identified as significant bottlenecks in yeast expression systems, pinpointing a major target for strain optimization. At the same time, it has become obvious that P. pastoris, as an evolutionarily more 'ancient' yeast, may in some cases be a better model for human cell biology and disease than Saccharomyces cerevisiae.
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