Genetic engineering of Pichia pastoris to humanize N-glycosylation of proteins.
The yeast Pichia pastoris is used extensively as the host cell for large-scale production of secreted recombinant proteins. Many proteins of pharmaceutical importance are N-glycosylated, and therefore require an expression host that yields N-linked oligosaccharides that are structurally and functionally identical to the human counterpart. The recent report by Choi et al. describes the use of combinatorial genetic libraries to alter the N-glycosylation pathway in P. pastoris to yield N-linked oligosaccharides with hybrid structures that are the same as the intermediates of mammalian-protein N-glycosylation. In view of recent progress in this area, the production of complex human glycans in yeasts is anticipated.
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556-5670, USA. roger.k.bretthauer.1@nd.edu
Roger K
RK
Bretthauer
D006031:Glycosylation; D006801:Humans; D008364:Mannosyltransferases / Q000235:genetics; D009844:Oligosaccharides / Q000378:metabolism*; D010766:Phosphorylation; D010843:Pichia / Q000235:genetics* / Q000378:metabolism; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism*
D009844:Oligosaccharides; D011994:Recombinant Proteins; D008364:Mannosyltransferases