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Updated: Aug 28, 2025

Multicolor Flow Cytometry Analyses of Cellular Immune Response in Rhesus Macaques

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Published on: April 22, 2010

Decoding human-macaque interspecies differences in Fc-effector functions: The structural basis for CD16-dependent

William D Tolbert¹, Neelakshi Gohain², Paul G Kremer³

¹Infectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD, United States.

Frontiers in Immunology

|September 22, 2022

Summary

We studied the Fc gamma receptor III (FcγRIII) Ile/Val polymorphism in rhesus macaques. Macaque FcγRIII variants show altered IgG binding affinity influenced by glycan composition, impacting immunotherapy research.

Keywords:

CD16 Fc-effector function FcγRIII Val/Ile158 IgG1(Fc)- FcγRIII complex structure - function of RM FcγRIII Ile/Val 158 Rhesus macaques Macaca mulatta

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Gene Editing of Primary Rhesus Macaque B Cells

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Published on: February 10, 2023

Area of Science:

Immunology
Structural Biology
Pharmacology

Background:

Fc-mediated effector functions are crucial for antibody immunotherapies and vaccine efficacy.
Assessing these functions in animal models is challenging due to species-specific immune system differences.
Rhesus macaques (Macaca mulatta) offer a relevant model but have unique Fc receptor (FcR) profiles compared to humans.

Purpose of the Study:

To investigate the structure-function relationships of the Ile/Val158 polymorphism in macaque Fc gamma receptor III (FcγRIII).
To understand how glycan composition on antibodies and FcγRIII affects binding affinity in this polymorphism.
To provide insights for interpreting non-human primate studies and human FcγRIIIa research.

Main Methods:

Characterization of FcγRIII allelic variants (Ile158 and Val158) from rhesus macaques.
Analysis of IgG subclass binding affinities to FcγRIII variants under varying glycan conditions.
Structure-function analysis focusing on the Fc/FcγRIII interface and glycan interactions.

Main Results:

FcγRIII allelic variants exhibit significant differences in affinity for macaque IgG subclasses, modulated by glycan composition.
The Ile158 variant, unlike human FcγRIIIa, shows higher affinity, potentially due to altered glycan-glycan interactions.
Glycan modifications on FcγRIII disproportionately affect the Val158 variant, sometimes leading to higher affinity.

Conclusions:

The Ile/Val158 polymorphism in macaque FcγRIII has distinct structure-function properties compared to humans.
Glycan composition plays a critical role in modulating FcγRIII-IgG interactions in macaques.
These findings are essential for accurate interpretation of macaque models in immunotherapy and vaccine development.