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...
Saved in:
Published in | Biochemistry Vol. 81; no. 8; pp. 835 - 857 |
---|---|
Main Authors | , , , , , |
Format | Journal Article Book Review |
Language | English |
Published |
Moscow
Pleiades Publishing
01.08.2016
Springer Springer Nature B.V |
Subjects | |
Online Access | Get full text |
Cover
Loading…
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. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-3 ObjectType-Review-1 |
ISSN: | 0006-2979 1608-3040 |
DOI: | 10.1134/S0006297916080058 |