Structure determination of N-linked oligosaccharides engineered at the CH1 domain of humanized LL2 |
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Authors: | Qu, Zhengxing Sharkey, Robert M. Hansen, Hans J. Goldenberg, David M. Leung, Shui-on |
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Affiliation: | Immunomedics, Inc, 300 American Road, Morris Plains, NJ 07950, USA 1The Garden State Cancer Center 520 Belleville Avenue, Belleville, NJ 07109, USA |
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Abstract: | Two humanized antibody mutants, hLL2HCN1 and hLL2HCN5, engineeredwith CH1 domain-appended carbohydrates (CHOs) were generatedto facilitate site-specific conjugation of radionudides andanti-cancer drugs to antibodies. Such site-specific conjugationmay minimize the incidence of immunoreactlvity perturbationas is often observed with random conjugation. Since the compositionsand structures of CHOs are important in determining the chemistry,efficiency, and extent of conjugation, the sequences of theCH1-appended CHOs were determined by exoglycosidase digestionsand fluorophore-assisted CHO electrophoresis (FACE). The CHOspecies attached at HCN1 and HCN5 sites in hLL2HCN1 and IJLL2HCN5,respectively, were distinct from each other, heterogeneous,and extensively processed. All of these CHOs were corefucosylatedcomplex-type oligosaccharides and contained Gal (galactose)and GlcNAc (N-acetylglucosamine) residues in the outer branches.Some of the outer branches were composed of Gal |
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