Sweet factory: an O-glycosylation competent Escherichia coli strain for the recombinant expression of complex biopharmaceuticals
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Date
2019-09-24
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Dissertation
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Abstract
Glycosylation represents an important modification influencing the quality of recombinant expressed biopharmaceuticals by modulating the stability and activity of commercially relevant therapeutics. As a result, the importance of E. coli as a manufacturing platform has continuously decreased due to the lack of post-translational modifications during protein expression. The presented E. coli-based expression system was established to achieve mucin-type O-glycosylation in vivo combining the expression of the human glycosyltransferase GalNAc-T2 and the uridine 5’diphospho-N-acetylglucosamine (UDP-GlcNAc) 4-epimerase derived from Plesiomonas shigelloides (WbgU). T7Muc10, a synthetic protein with multiple glycosylation sites, and the granulocyte-colony stimulating factor G-CSF, a pharmaceutically relevant product, were included as potential target proteins.
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Faculties
Medizinische Fakultät
Institutions
UKU. Institut für Pharmakologie und Toxikologie
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DFG Project uulm
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Keywords
G-CSF, Escherichia coli, Protein expression, Glycosyltransferase GalNAc-T2, UDP-GlcNAc 4-epimerase WbgU, Chaperone co-expression, Mucin-type O-glycoslyation, Escherichia coli, Glykosylierung, Glycosyltransferasen, Escherichia coli, Gene expression, Glycosylation, Recombinant proteins, Glycoproteins, Glycosyltransferases, DDC 570 / Life sciences, DDC 610 / Medicine & health