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MAbs. 2017 Jul;9(5):767-773. doi: 10.1080/19420862.2017.1323159. Epub 2017 May 2.

Affinity of human IgG subclasses to mouse Fc gamma receptors.

Author information

1
a Department of Experimental Immunohematology , Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam , The Netherlands.
2
b Department of Transfusion Medicine , Bloodworks Northwest Research Institute , Seattle , Washington , USA.
3
c Department of Immunopathology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center , University of Amsterdam , The Netherlands.

Abstract

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.

KEYWORDS:

Fc-receptors; FcγR; IgG subclasses; mouse models; surface plasmon resonance

PMID:
28463043
PMCID:
PMC5524164
DOI:
10.1080/19420862.2017.1323159
[Indexed for MEDLINE]
Free PMC Article

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