效应器
单克隆抗体
功能(生物学)
计算生物学
生物
受体
抗体
Fc受体
细胞生物学
碎片结晶区
信号转导
免疫系统
癌症治疗
糖基化
抗体依赖性细胞介导的细胞毒性
免疫疗法
癌症免疫疗法
癌症
免疫学
生物化学
遗传学
作者
Rena Liu,Robert J. Oldham,Emma Teal,Stephen A. Beers,Mark S. Cragg
出处
期刊:Antibodies
[MDPI AG]
日期:2020-11-17
卷期号:9 (4): 64-64
被引量:101
摘要
The majority of monoclonal antibody (mAb) therapeutics possess the ability to engage innate immune effectors through interactions mediated by their fragment crystallizable (Fc) domain. By delivering Fc-Fc gamma receptor (FcγR) and Fc-C1q interactions, mAb are able to link exquisite specificity to powerful cellular and complement-mediated effector functions. Fc interactions can also facilitate enhanced target clustering to evoke potent receptor signaling. These observations have driven decades-long research to delineate the properties within the Fc that elicit these various activities, identifying key amino acid residues and elucidating the important role of glycosylation. They have also fostered a growing interest in Fc-engineering whereby this knowledge is exploited to modulate Fc effector function to suit specific mechanisms of action and therapeutic purposes. In this review, we document the insight that has been generated through the study of the Fc domain; revealing the underpinning structure-function relationships and how the Fc has been engineered to produce an increasing number of antibodies that are appearing in the clinic with augmented abilities to treat cancer.
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