Cytoplasmic GlycoengineeringAuthor(s): Emma Freky
Glycosylation of proteins significantly impacts their physical and organic properties. However, our capacity to design novel glycoprotein structures stays restricted. Set up bacterial glycoengineering stages require emission of the acceptor protein to the periplasmic space and preassembly of the oligosaccharide substrate as a lipid-connected forerunner, restricting admittance to protein and glycan substrates separately. Here, we bypass these bottlenecks by fostering an effortless glycoengineering stage that works in the bacterial cytoplasm. The Glycolic stage uses an as of late found site-explicit polypeptide glycosyltransferase along with variable glycosyltransferase modules to integrate characterized glycans, of the bacterial or mammalian beginning, straightforwardly onto recombinant proteins in the E. coli cytoplasm.