O-linked glycosylation is a post-translational event where O-linked glycans attach to a polypeptide mainly through a glycosidic bond between the terminal monosaccharide residue and the OH group of serine or threonine residues. O-linked glycosylation may also occur through tyrosine, hydroxylysine, or hydroxyproline residues. O-glycans plays an important role in many biological processes: (i) protect the epithelial cells at the apical membrane from hostile environmental factors; (ii) block infection by pathogens; (iii) participate in cellular signaling events and so on. Unlike N-glycans, there is no known O-linked amino acid consensus sequence yet. The O-glycans are structurally diverse and they can be divided into several structural families with relatively heterogeneous core structures.
Figure 1. O-glycans are linked to a subset of serines or threonines.
More than 60% of therapeutic proteins are post-translationally modified following biosynthesis by the addition of N-glycans or O-glycans. It is necessary to characterize glycans in efficient manufacturing processes so as to maintain continued biotherapeutics glycosylation patterns. At Creative Proteomics, we provide o-glycan profiling service to support the development and commercialization of therapeutic proteins. The workflow of our O-glycan profiling analysis is as follows.
Figure 2. Workflow for O-glycan profiling service.
We work with a range of sample sources as follows.
As one of the leading companies in the proteomics field with decades of experience, Creative Proteomics provides glycomics analysis service customized to your needs. Please contact us to discuss your project.
1. Zhang L, Luo S, Zhang B. Glycan analysis of therapeutic glycoproteins//MAbs. Taylor & Francis, 2016, 8(2): 205-215.