Functional role of carbohydrate residues in human immunoglobulin G and therapeutic monoclonal antibodies

Therapeutic monoclonal antibodies (TMA) provide an important means for treating diseases that were previously considered untreatable. Currently more than 40 full-size TMAs created primarily based on immunoglobulin G1 are widely used for treating various illnesses. Glycosylation of TMA is among other...

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Published inBiochemistry Vol. 81; no. 8; pp. 835 - 857
Main Authors Dorokhov, Y. L., Sheshukova, E. V., Kosobokova, E. N., Shindyapina, A. V., Kosorukov, V. S., Komarova, T. V.
Format Journal Article Book Review
LanguageEnglish
Published Moscow Pleiades Publishing 01.08.2016
Springer
Springer Nature B.V
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Summary:Therapeutic monoclonal antibodies (TMA) provide an important means for treating diseases that were previously considered untreatable. Currently more than 40 full-size TMAs created primarily based on immunoglobulin G1 are widely used for treating various illnesses. Glycosylation of TMA is among other numerous factors that affect their biological activity, effector functions, immunogenicity, and half-life in the patient’s serum. The importance of carbohydrate residues for activity of human serum immunoglobulin and TMA produced in animal cells is considered in this review, with emphasis given to N-glycosylation of the Fc fragment of the antibody.
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ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297916080058