Effect of glycosylation on antibody function: implications for genetic engineering.
Effect of glycosylation on antibody function: implications for genetic engineering.
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DOI：
10.1016/s0167-7799(96)10062-7
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发表时间：
1997
影响因子：
17.3
通讯作者：
A. Wright;S. Morrison
中科院分区：
文献类型：
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作者：
A. Wright;S. Morrison
抗体既能够结合抗原，又能够引发反应，将抗原从循环中消除。所有抗体在其恒定区的保守位置处被糖基化，碳水化合物的存在对于补体激活等抗原清除功能至关重要。附着的碳水化合物的结构也会影响抗体活性。抗体糖基化可能受到产生抗体的细胞、抗体构象和细胞培养条件的影响。在设计和生产具有选定特异性和功能的抗体时应考虑这些变量。
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.