Found 1 structure.
Displayed structure 1
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1. Compound ID: 20387
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a-D-Manp-(1-6)-+
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a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/(->4) Asn-X-Ser/Thr (protein) | pp-Dol/ |
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Structure type: oligomer
Aglycon: (->4) Asn-X-Ser/Thr (protein) | pp-Dol
Compound class: N-glycan, mannan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85
The structure is contained in the following publication(s):
- Article ID: 8093
Anyaogu DC, Mortensen UH "Manipulating the glycosylation pathway in bacterial and lower eukaryotes for production of therapeutic proteins" -
Current Opinion in Biotechnology 36 (2015) 122-128
The medical use of pharmaceutical proteins is rapidly increasing and cheap, fast and efficient production is therefore attractive. Microbial production hosts are promising candidates for development and production of pharmaceutical proteins. However, as most therapeutic proteins are secreted proteins, they are frequently N-glycosylated. This hampers production in microbes as these hosts glycosylate proteins differently. The resulting products may therefore be immunogenic, unstable and show reduced efficacy. Recently, successful glycoengineering of microbes has demonstrated that it is possible to produce proteins with humanlike glycan structures setting the stage for production of pharmaceutical proteins in bacteria, yeasts and algae.
oligosaccharyltransferase, N-glycosylation, glycoengineer, humanization
NCBI PubMed ID: 26340101Publication DOI: 10.1016/j.copbio.2015.08.012Journal NLM ID: 9100492Publisher: London: Elsevier
Correspondence: Mortensen UH
Institutions: Division for Microbiology and Production, National Food Institute, Technical University of Denmark, Kongens Lyngby, Denmark, Section for Eukaryotic Biotechnology, Department of Systems Biology, Technical University of Denmark, Kongens Lyngby, Denmark
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