Remodeling of glycoprotein and carbohydrate antigens.
Glycosylation is the most extensive of all post-translational modifications in proteins. It has important functions in their secretion, antigenicity and metabolic clearance through structural polymorphism. In recent years, advances in recombinant DNA technology allowed the production of recombinant therapeutic proteins, among which glycosylated proteins displayed differences compared to their native counterparts, including antigenic carbohydrates. In this review, we discuss the potential use of cloned glycosyltransferases in remodeling recombinant glycoprotein antigens as well as in synthesizing tumor-associated carbohydrate antigens.
Laboratoire de Neurobiologie, Centre National de la Recherche Scientifique, Marseille, France.
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D000941:Antigens / Q000737:chemistry*; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D006801:Humans; D007167:Immunotherapy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015202:Protein Engineering
D000941:Antigens; D002241:Carbohydrates; D006023:Glycoproteins