受体
抗体
免疫球蛋白G
免疫学
Fc受体
化学
子类
免疫球蛋白Fc片段
生物
生物化学
作者
Gillian Dekkers,Arthur E. H. Bentlage,Tamara C. Stegmann,Heather L. Howie,Suzanne N. Lissenberg‐Thunnissen,James C. Zimring,Theo Rispens,Gestur Vidarsson
出处
期刊:mAbs
[Landes Bioscience]
日期:2017-05-02
卷期号:9 (5): 767-773
被引量:288
标识
DOI:10.1080/19420862.2017.1323159
摘要
Human IgG is the main antibody class used in antibody therapies because of its efficacy and longer half-life, which are completely or partly due to FcγR-mediated functions of the molecules. Preclinical testing in mouse models are frequently performed using human IgG, but no detailed information on binding of human IgG to mouse FcγRs is available. The orthologous mouse and human FcγRs share roughly 60-70% identity, suggesting some incompatibility. Here, we report binding affinities of all mouse and human IgG subclasses to mouse FcγR. Human IgGs bound to mouse FcγR with remarkably similar binding strengths as we know from binding to human ortholog receptors, with relative affinities IgG3>IgG1>IgG4>IgG2 and FcγRI>>FcγRIV>FcγRIII>FcγRIIb. This suggests human IgG subclasses to have similar relative FcγR-mediated biological activities in mice.
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