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    Molecular Basis of Broad Spectrum N-Glycan Specificity and Processing of Therapeutic IgG Monoclonal Antibodies by Endoglycosidase S2

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    Author
    Klontz, E.H.
    Trastoy, B.
    Deredge, D.
    Date
    2019
    Journal
    ACS Central Science
    Publisher
    American Chemical Society
    Type
    Article
    
    Metadata
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    See at
    https://dx.doi.org/10.1021/acscentsci.8b00917
    Abstract
    Immunoglobulin G (IgG) glycosylation critically modulates antibody effector functions. Streptococcus pyogenes secretes a unique endo-β-N-acetylglucosaminidase, EndoS2, which deglycosylates the conserved N-linked glycan at Asn297 on IgG Fc to eliminate its effector functions and evade the immune system. EndoS2 and specific point mutants have been used to chemoenzymatically synthesize antibodies with customizable glycosylation for gain of functions. EndoS2 is useful in these schemes because it accommodates a broad range of N-glycans, including high-mannose, complex, and hybrid types; however, its mechanism of substrate recognition is poorly understood. We present crystal structures of EndoS2 alone and bound to complex and high-mannose glycans; the broad N-glycan specificity is governed by critical loops that shape the binding site of EndoS2. Furthermore, hydrolytic experiments, domain-swap chimeras, and hydrogen-deuterium exchange mass spectrometry reveal the importance of the carbohydrate-binding module in the mechanism of IgG recognition by EndoS2, providing insights into engineering enzymes to catalyze customizable glycosylation reactions. Copyright 2019 American Chemical Society.
    Keyword
    IgG antibodies
    EndoS2
    endoglycosidase S2
    endoglycosidase enzymes
    N-linked glycan
    Immunoglobulin G
    Polysaccharides
    Identifier to cite or link to this item
    https://www.scopus.com/inward/record.uri?eid=2-s2.0-85061524266&doi=10.1021%2facscentsci.8b00917&partnerID=40&md5=ca733852e1c2d866aa920f36321d6eb1; http://hdl.handle.net/10713/8694
    ae974a485f413a2113503eed53cd6c53
    10.1021/acscentsci.8b00917
    Scopus Count
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    UMB Open Access Articles 2019

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