title: Engineering yeast for producing human glycoproteins: where are we now?
abstract: Yeast has advanced as an alternative for mammalian cell culture for the production of recombinant therapeutic glycoproteins. Engineered yeast strains not only allow to mimic the human N-glycosylation pathway but also specific types of human O-glycosylation. This is of great value for therapeutic protein production and indispensable to determine the structure-function relationships of glycans on recombinant proteins. However, as the technology matures, some limitations have come up that may hamper biomedical applications and must be considered to exploit the full potential of the unprecedented glycan homogeneity obtained on relevant biopharmaceuticals. In this special report, we focus on the recent developments in N- and O-glycosylation engineering in yeasts of industrial importance, to produce recombinant therapeutics with customized glycans.
authors.affiliation: Unit for Medical Biotechnology, Inflammation Research Centre (IRC), VIB-UGent, Technologiepark 927, B-9052 Ghent-Zwijnaarde, Belgium.
authors.forename: Bram
authors.initials: B
authors.lastname: Laukens
authors.forename: Charlotte
authors.initials: C
authors.lastname: De Visscher
authors.forename: Nico
authors.initials: N
authors.lastname: Callewaert
mesh_terms: D005818:Genetic Engineering; D006023:Glycoproteins / Q000096:biosynthesis* / Q000627:therapeutic use; D006031:Glycosylation; D006801:Humans; D030781:Organisms, Genetically Modified; D011134:Polysaccharides; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000627:therapeutic use; D012441:Saccharomyces cerevisiae / Q000235:genetics; D015003:Yeasts / Q000235:genetics*
chemical_list: D006023:Glycoproteins; D011134:Polysaccharides; D011994:Recombinant Proteins
keywords: N-glycosylation engineering; O-glycosylation engineering; Pichia pastoris; Saccharomyces cerevisiae; therapeutic proteins; yeast