REVIEW: Functional Role of Carbohydrate Residues in Human Immunoglobulin G and Therapeutic Monoclonal Antibodies

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Y. L. Dorokhov^1,2*, E. V. Sheshukova¹, E. N. Kosobokova¹, A. V. Shindyapina^1,2, V. S. Kosorukov¹, and T. V. Komarova^1,2

¹Vavilov Institute of General Genetics, Russian Academy of Sciences, 119991 Moscow, Russia; fax: +7 (499) 132-8962

²Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: +7 (495) 939-3181; E-mail: dorokhov@genebee.msu.su

^* To whom correspondence should be addressed.

Received April 28, 2016; Revision received May 27, 2016

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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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KEY WORDS: monoclonal antibody, immunoglobulin G, glycosylation, antibody-dependent cell cytotoxicity, Chinese hamster ovary cells, immunotherapy, biosimilarity

DOI: 10.1134/S0006297916080058

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