Abstract: The present invention relates to recombinant polypeptide therapeutics having an engineered O-linked amino acid (AA) glycosylation sequence (motif), which is covalently linked to O-glycan(s) (tag). Recombinant O-glycosylated polypeptides may be produced in mammalian cells to present natural or un-natural O-glycan structures through metabolic labelling.

Abstract: The disclosure provides compositions and methods that make use of a target protein that is capable of binding to a small molecule in order to form a complex, and a binding member that specifically binds to the complex, wherein the target protein is derived from a non-human protein and the small molecule is an inhibitor of the non-human protein. The non-human protein may be derived from a viral, bacterial, fungal or protozoal protein. These compositions and methods permit the controlled interaction of polypeptides that are individually fused to the target protein and binding member, respectively, and can be used to control the activity of dimerization-inducible proteins such as split transcription factors and split chimeric antigen receptors through the addition of the small molecule. The disclosure provides expression vectors, binding members, dimerization-inducible proteins, nucleic acids, cells, viral particles, kits, systems and methods that involve these components.

Abstract: The present invention relates to recombinant polypeptide therapeutics having an engineered O-linked amino acid (AA) glycosylation sequence (motif), which is covalently linked to O-glycan(s) (tag). Recombinant O-glycosylated polypeptides may be produced in mammalian cells to present natural or un-natural O-glycan structures through metabolic labelling.