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Crowley AR, Osei-Owusu NY, Dekkers G, et al. Biophysical Evaluation of Rhesus Macaque Fc Gamma Receptors Reveals Similar IgG Fc Glycoform Preferences to Human Receptors. Front Immunol. 2021;12:754710doi: 10.3389/fimmu.2021.754710.
Crowley, A. R., Osei-Owusu, N. Y., Dekkers, G., Gao, W., Wuhrer, M., Magnani, D. M., Reimann, K. A., Pincus, S. H., Vidarsson, G., & Ackerman, M. E. (2021). Biophysical Evaluation of Rhesus Macaque Fc Gamma Receptors Reveals Similar IgG Fc Glycoform Preferences to Human Receptors. Frontiers in immunology, 12754710. https://doi.org/10.3389/fimmu.2021.754710
Crowley, Andrew R, et al. "Biophysical Evaluation of Rhesus Macaque Fc Gamma Receptors Reveals Similar IgG Fc Glycoform Preferences to Human Receptors." Frontiers in immunology vol. 12 (2021): 754710. doi: https://doi.org/10.3389/fimmu.2021.754710
Crowley AR, Osei-Owusu NY, Dekkers G, Gao W, Wuhrer M, Magnani DM, Reimann KA, Pincus SH, Vidarsson G, Ackerman ME. Biophysical Evaluation of Rhesus Macaque Fc Gamma Receptors Reveals Similar IgG Fc Glycoform Preferences to Human Receptors. Front Immunol. 2021 Oct 12;12:754710. doi: 10.3389/fimmu.2021.754710. eCollection 2021. PMID: 34712242; PMCID: PMC8546228.
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Front Immunol. 2021 Oct 12;12:754710. doi: 10.3389/fimmu.2021.754710. eCollection 2021.

Biophysical Evaluation of Rhesus Macaque Fc Gamma Receptors Reveals Similar IgG Fc Glycoform Preferences to Human Receptors.

Frontiers in immunology

Andrew R Crowley, Nana Yaw Osei-Owusu, Gillian Dekkers, Wenda Gao, Manfred Wuhrer, Diogo M Magnani, Keith A Reimann, Seth H Pincus, Gestur Vidarsson, Margaret E Ackerman

Affiliations

  1. Department of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Dartmouth College, Hanover, NH, United States.
  2. Sanquin Research and Landsteiner Laboratory, Academic Medical Centre, Department of Experimental Immunohematology, University of Amsterdam, Amsterdam, Netherlands.
  3. Antagen Pharmaceuticals Inc., Boston, MA, United States.
  4. Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, Netherlands.
  5. Nonhuman Primate Reagent Resource, MassBiologics of the University of Massachusetts Medical School, Boston, MA, United States.
  6. Department of Microbiology, Immunology and Parasitology, Louisiana State University Health Sciences Center, New Orleans, LA, United States.
  7. Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT, United States.
  8. Thayer School of Engineering, Dartmouth College, Hanover, NH, United States.

PMID: 34712242 PMCID: PMC8546228 DOI: 10.3389/fimmu.2021.754710

Abstract

Rhesus macaques are a common non-human primate model used in the evaluation of human monoclonal antibodies, molecules whose effector functions depend on a conserved N-linked glycan in the Fc region. This carbohydrate is a target of glycoengineering efforts aimed at altering antibody effector function by modulating the affinity of Fcγ receptors. For example, a reduction in the overall core fucose content is one such strategy that can increase antibody-mediated cellular cytotoxicity by increasing Fc-FcγRIIIa affinity. While the position of the Fc glycan is conserved in macaques, differences in the frequency of glycoforms and the use of an alternate monosaccharide in sialylated glycan species add a degree of uncertainty to the testing of glycoengineered human antibodies in rhesus macaques. Using a panel of 16 human IgG1 glycovariants, we measured the affinities of macaque FcγRs for differing glycoforms

Copyright © 2021 Crowley, Osei-Owusu, Dekkers, Gao, Wuhrer, Magnani, Reimann, Pincus, Vidarsson and Ackerman.

Keywords: ADCC - antibody dependent cellular cytotoxicity; Fc gamma receptor; IgG; N glycan; complement dependent cytotoxicity ; nonhuman primate; phagocytosis; rhesus macaque

Conflict of interest statement

WG was employed by Antagen Pharmaceuticals Inc. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a p

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