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.