title: Pichia pastoris: protein production host and model organism for biomedical research.
abstract: 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.
authors: University of Natural Resources & Life Sciences (BOKU), Department of Biotechnology, 1190 Vienna, Austria.
authors: Brigitte
authors: B
authors: Gasser
authors: Roland
authors: R
authors: Prielhofer
authors: Hans
authors: H
authors: Marx
authors: Michael
authors: M
authors: Maurer
authors: Justyna
authors: J
authors: Nocon
authors: Matthias
authors: M
authors: Steiger
authors: Verena
authors: V
authors: Puxbaum
authors: Michael
authors: M
authors: Sauer
authors: Diethard
authors: D
authors: Mattanovich
mesh_terms: D035843:Biomedical Research / Q000379:methods*; D001709:Biotechnology / Q000379:methods*; D005818:Genetic Engineering / Q000379:methods; D005827:Genetics, Microbial / Q000379:methods; D006801:Humans; D010843:Pichia / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013678:Technology, Pharmaceutical / Q000379:methods*
chemical_list: D011994:Recombinant Proteins