Manipulating the glycosylation pathway in bacterial and lower eukaryotes for production of therapeutic proteins.
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.
Division for Microbiology and Production, National Food Institute, Technical University of Denmark, 2800 Kongens Lyngby, Denmark.
Diana Chinyere
DC
Anyaogu
Section for Eukaryotic Biotechnology, Department of Systems Biology, Søltofts Plads, Building 223, Technical University of Denmark, 2800 Kongens Lyngby, Denmark. Electronic address: um@bio.dtu.dk.
Uffe Hasbro
UH
Mortensen
D000818:Animals; D056890:Eukaryota / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D011134:Polysaccharides / Q000378:metabolism; D015202:Protein Engineering; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*
D011134:Polysaccharides; D011506:Proteins