title: Quo vadis? The challenges of recombinant protein folding and secretion in Pichia pastoris.
abstract: The development of Pichia pastoris as a production platform for recombinant proteins has been a remarkable success story over the last three decades. Stable cheap production processes and the good protein secretion abilities were pacemakers of this development. However, limitations of protein folding, glycosylation or secretion have been identified quite early on. With the availability of genome sequences and the development of systems biology characterization in the last 5 years, remarkable success in strain improvement was achieved. Here, we focus on recent developments of characterization and improvement of P. pastoris production strains regarding protein folding, intracellular trafficking, glycosylation and proteolytic degradation.
authors.affiliation: Austrian Centre of Industrial Biotechnology, Muthgasse 11, 1190, Vienna, Austria.
authors.forename: Verena
authors.initials: V
authors.lastname: Puxbaum
authors.forename: Diethard
authors.initials: D
authors.lastname: Mattanovich
authors.forename: Brigitte
authors.initials: B
authors.lastname: Gasser
mesh_terms: D060746:Endoplasmic Reticulum-Associated Degradation; D005089:Exocytosis; D006031:Glycosylation; D006056:Golgi Apparatus / Q000378:metabolism; D010843:Pichia / Q000235:genetics / Q000378:metabolism*; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D021381:Protein Transport; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D056811:Unfolded Protein Response / Q000502:physiology; D014617:Vacuoles / Q000378:metabolism
chemical_list: D011134:Polysaccharides; D011994:Recombinant Proteins