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Protein endoglycosidases are useful for biocatalytic alteration of glycans on protein surfaces, but the currently limited selectivity of endoglycosidases has prevented effective manipulation of certain N-linked glycans widely found in nature. Here we reveal that a bacterial endoglycosidase from Streptococcus pyogenes , EndoS, is complementary to other known endoglycosidases (EndoA, EndoH) used for current protein remodeling. It allows processing of complex-type N-linked glycans +/- core fucosylation but does not process oligomannose- or hybrid-type glycans. This biocatalytic activity now addresses previously refractory antibody glycoforms.

Original publication




Journal article


J Am Chem Soc

Publication Date





8030 - 8033


Glycoproteins, Glycoside Hydrolases, Humans, Immunoglobulin G, Models, Molecular, Polysaccharides, Protein Conformation, Streptococcus pyogenes, Substrate Specificity