Effect of glycosylation on antibody function: implications for genetic engineering.
Antibodies are able to both bind antigens and trigger the responses that eliminate them from circulation. All antibodies are glycosylated at conserved positions in their constant regions, and the presence of carbohydrate can be critical for antigen clearance functions such as complement activation. The structure of the attached carbohydrate can also affect antibody activity. Antibody glycosylation can be influenced by the cell in which it is produced, the conformation of the antibody and cell culture conditions. These variables should be considered in the design and production of antibodies with selected specificity and function.
Wright
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Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90095, USA.
Morrison
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SL
D000906:Antibodies / Q000235:genetics / Q000276:immunology*; D000918:Antibody Specificity; D002236:Carbohydrate Conformation; D002241:Carbohydrates / Q000737:chemistry / Q000502:physiology; D003001:Cloning, Molecular; D006031:Glycosylation; D006801:Humans; D007074:Immunoglobulin G / Q000235:genetics / Q000276:immunology; D011994:Recombinant Proteins / Q000235:genetics / Q000276:immunology
D000906:Antibodies; D002241:Carbohydrates; D007074:Immunoglobulin G; D011994:Recombinant Proteins