@article { ISI:000460048700006,
	title = {A Bacterial Expression Platform for Production of Therapeutic Proteins Containing Human-like O-Linked Glycans},
	journal = {CELL CHEMICAL BIOLOGY},
	volume = {26},
	number = {2},
	year = {2019},
	month = {FEB 21},
	pages = {203+},
	abstract = {We have developed an Escherichia coli strain for the in vivo production of O-glycosylated proteins. This was achieved using a dual plasmid approach: one encoding a therapeutic protein target, and a second encoding the enzymatic machinery required for O-glycosylation. The latter plasmid encodes human polypeptide N-acetylgalactosaminyl transferase as well as a beta 1,3-galactosyl transferase and UDP-Glc (NAc)-4-epimerase, both from Campylobacter jejuni, and a disulfide bond isomerase of bacterial or human origin. The effectiveness of this two-plasmid synthetic operon system has been tested on three proteins with therapeutic potential: the native and an engineered version of the naturally O-glycosylated human interferon alpha-2b, as well as human growth hormone with one engineered site of glycosylation. Having established proof of principle for the addition of the core-1 glycan onto proteins, we are now developing this system as a platform for producing and modifying human protein therapeutics with more complex O-glycan structures in E. coli.},
	issn = {2451-9448},
	doi = {10.1016/j.chembiol.2018.10.017},
	author = {Du, Ting and Buenbrazo, Nakita and Kell, Laura and Rahmani, Sadia and Sim, Lyann and Withers, Stephen G. and DeFrees, Shawn and Wakarchuk, Warren}
}
