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- aggregation classification "A1".
- aggregation creator B674364.
- aggregation creator B674365.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2012".
- aggregation format "application/pdf".
- aggregation hasFormat 2968147.bibtex.
- aggregation hasFormat 2968147.csv.
- aggregation hasFormat 2968147.dc.
- aggregation hasFormat 2968147.didl.
- aggregation hasFormat 2968147.doc.
- aggregation hasFormat 2968147.json.
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- aggregation hasFormat 2968147.txt.
- aggregation hasFormat 2968147.xls.
- aggregation hasFormat 2968147.yaml.
- aggregation isPartOf urn:issn:1932-6203.
- aggregation language "eng".
- aggregation rights "I have retained and own the full copyright for this publication".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Engineering Yarrowia lipolytica to produce glycoproteins homogeneously modified with the universal Man(3)GlcNAc(2) N-glycan core".
- aggregation abstract "Yarrowia lipolytica is a dimorphic yeast that efficiently secretes various heterologous proteins and is classified as "generally recognized as safe." Therefore, it is an attractive protein production host. However, yeasts modify glycoproteins with non-human high mannose-type N-glycans. These structures reduce the protein half-life in vivo and can be immunogenic in man. Here, we describe how we genetically engineered N-glycan biosynthesis in Yarrowia lipolytica so that it produces Man(3)GlcNAc(2) structures on its glycoproteins. We obtained unprecedented levels of homogeneity of this glycanstructure. This is the ideal starting point for building human-like sugars. Disruption of the ALG3 gene resulted in modification of proteins mainly with Man(5)GlcNAc(2) and GlcMan(5)GlcNAc(2) glycans, and to a lesser extent with Glc(2)Man(5)GlcNAc(2) glycans. To avoid underoccupancy of glycosylation sites, we concomitantly overexpressed ALG6. We also explored several approaches to remove the terminal glucose residues, which hamper further humanization of N-glycosylation; overexpression of the heterodimeric Apergillus niger glucosidase II proved to be the most effective approach. Finally, we overexpressed an alpha-1,2-mannosidase to obtain Man(3)GlcNAc(2) structures, which are substrates for the synthesis of complex-type glycans. The final Yarrowia lipolytica strain produces proteins glycosylated with the trimannosyl core N-glycan (Man(3)GlcNAc(2)), which is the common core of all complex-type N-glycans. All these glycans can be constructed on the obtained trimannosyl N-glycan using either in vivo or in vitro modification with the appropriate glycosyltransferases. The results demonstrate the high potential of Yarrowia lipolytica to be developed as an efficient expression system for the production of glycoproteins with humanized glycans.".
- aggregation authorList BK1035958.
- aggregation issue "6".
- aggregation volume "7".
- aggregation aggregates 2968250.
- aggregation isDescribedBy 2968147.
- aggregation similarTo journal.pone.0039976.
- aggregation similarTo LU-2968147.