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J Immunol Methods. 1998 Apr 15;213(2):131-44.

Carbohydrates engineered at antibody constant domains can be used for site-specific conjugation of drugs and chelates.

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Immunomedics, Morris Plains, NJ 07950, USA.


To improve the efficiency of site-specific conjugation of chelates and drugs to antibodies, and to minimize the incidence of immunoreactivity perturbation to the resultant immunoconjugates, Asn-linked oligosaccharide moieties were designed and engineered into the constant domains of a humanized anti-CD22 monoclonal antibody, hLL2. From 10 potential glycosylation mutants, two CH1 domain glycosylation sites, HCN1 and HCN5, were identified that were positioned favorably for glycosylation. The carbohydrate (CHO) chains attached at these sites were differentially processed so that HCN5-CHOs were physically larger than HCN1-CHOs. Although both the CH1-appended CHOs, and the LL2 Vkappa-appended CHOs conjugated efficiently with small chelates, the HCN5-CHOs, due to the structural and positional superiority, appear to be a better conjugation site for large drug complexes, such as 18 kDa doxorubicin (DOX)-dextran.

[Indexed for MEDLINE]

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