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Cited by 87Monoclonal and Polyclonal Antibodies ResearchT-cell and B-cell ImmunologyImmune Cell Function and Interaction

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Improving Antibody Therapeutics by Manipulating the Fc Domain: Immunological and Structural Considerations

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Delidakis, George, Kim, Jin Eyun, George, Katia, Georgiou, George·2022·Annual Review of Biomedical Engineering
DOI 10.1146/annurev-bioeng-082721-024500PMC PMC9648538
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Abstract

Interactions between the crystallizable fragment (Fc) domain of antibodies and a plethora of cellular Fc receptors (FcRs) or soluble proteins form a critical link between humoral and innate immunity. In particular, the immunoglobulin G Fc domain is critical for the clearance of target cells by processes that include ( a) cytotoxicity, phagocytosis, or complement lysis; ( b) modulation of inflammation; ( c) antigen presentation; ( d) antibody-mediated receptor clustering; and ( e) cytokine release. More than 30 Fc-engineered antibodies aimed primarily at tailoring these effects for optimal therapeutic outcomes are in clinical evaluation or have already been approved. Nonetheless, our understanding of how FcR engagement impacts various immune cell phenotypes is still largely incomplete. Recent insights into FcR biology coupled with advances in Fc:FcR structural analysis, Fc engineering, and mouse models that recapitulate human biology are helping to fill in existing knowledge gaps. These advances will provide a blueprint on how to fine-tune the Fc domain to achieve optimal therapeutic efficacy.

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  • Tissue IgG levels are regulated through FcRn (Fcgrt-encoded) receptor-mediated recycling, depletion of which reduces tissue IgG levels.

    “Tissue IgG levels are regulated through FcRn (Fcgrt-encoded) receptor-mediated recycling, the depletion of which is known to reduce tissue IgG levels.54”

    From Spatial transcriptomic landscape unveils immunoglobin-associated senescence as a hallmark of aging (2024) · cites this paper as [54]

    “The Neonatal FcR” section says FcRn recycles IgG, protects it from degradation, and transports it across epithelial barriers. “Engineering Binding to FcRn” reports that interfering with recycling reduces circulating pathogenic autoantibodies. The copy does not report that FcRn depletion reduces tissue IgG levels or identify FcRn as Fcgrt-encoded (page numbers unavailable). (LLM, conf=0.85)

    Experimental — accuracy not yet measured

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Metadata

Authors
Delidakis, G., Kim, J. E., George, K., & Georgiou, G.
Affiliations
The University of Texas at Austin (US)
ORCID
Venue
Annual Review of Biomedical Engineering
Publisher
Annual Reviews
Published
2022-06-06
Volume
24
Issue
1
Pages
249-274
ISSN
  • 1523-9829 (ISSN-L)
  • 1545-4274
DOI
10.1146/annurev-bioeng-082721-024500
PMC
PMC9648538
OpenAlex
W4220826711
Cited by
87
References
5
Citations by year
2026: 25 · 2025: 19 · 2024: 28 · 2023: 14 · 2022: 1
FWCI
1.53
Type
journal article
Language
en
Open access
Licence
Locations
  • Annual Review of Biomedical Engineering (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Institute of Allergy and Infectious Diseases (U01AI148118)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Cell Function and Interaction
Keywords
therapeutic antibodies, Fc receptors, IgG, antibody-mediated phagocytosis, antibody-mediated cytotoxicity, complement-mediated lysis, inflammation modulation, antigen presentation, receptor clustering, cytokine production, mouse models of human disease
MeSH terms
Animals, Humans, Immunity, Innate, Immunoglobulin Fc Fragments, Phagocytosis, Receptors, Fc, Mice

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