Protein glycosylation is a fundamental process in living organisms. Vertebrate type O-glycans are desirable because of the potential for site-selectivity and the ability to incorporate a single GalNAc residue. The fact that the glycan is composed of a human sugar and linkage, specifically, GalNAcĪ±1-O-Ser/Thr, makes this modification ideal for use in therapeutic applications.
Dartmouth scientists have now demonstrated that a bacterial host cell expressing active UDP-GalNAc:UDP-GalNAc polypeptide transferase and active UDP-GlcNAc C-4 epimerase can efficiently O-glycosylate a recombinant mammalian protein expressed by the host cell. This finding now provides a facile prokaryotic system for synthesizing homogeneously O-glycosylated glycoproteins for use in commercial and therapeutic applications.
These findings are claimed in the published PCT Application No. PCT/US2010/060168. We are seeking an industrial partner to further refine and market this technology. (Ref: #J553)
