Type I and type II Fc receptors regulate innate and adaptive immunity.

Publisher: Nature America Inc Country of Publication: United States NLM ID: 100941354 Publication Model: Print Cited Medium: Internet ISSN: 1529-2916 (Electronic) Linking ISSN: 15292908 NLM ISO Abbreviation: Nat Immunol Subsets: MEDLINE

Original Publication: New York, NY : Nature America Inc. c2000-

Adaptive Immunity* ; Immunity, Innate*; Immunoglobulin Fc Fragments/*immunology ; Receptors, IgG/*immunology; Amino Acid Sequence ; Antibodies/immunology ; Antigen Presentation/immunology ; Autoimmune Diseases/immunology ; Glycosylation ; Humans ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fc Fragments/classification ; Immunoglobulin G/immunology ; Neoplasms/immunology ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, IgG/chemistry ; Receptors, IgG/classification ; Vaccination

Antibodies produced in response to a foreign antigen are characterized by polyclonality, not only in the diverse epitopes to which their variable domains bind but also in the various effector molecules to which their constant regions (Fc domains) engage. Thus, the antibody's Fc domain mediates diverse effector activities by engaging two distinct classes of Fc receptors (type I and type II) on the basis of the two dominant conformational states that the Fc domain may adopt. These conformational states are regulated by the differences among antibody subclasses in their amino acid sequence and by the complex, biantennary Fc-associated N-linked glycan. Here we discuss the diverse downstream proinflammatory, anti-inflammatory and immunomodulatory consequences of the engagement of type I and type II Fc receptors in the context of infectious, autoimmune, and neoplastic disorders.

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U19 AI109946 United States AI NIAID NIH HHS

0 (Antibodies)
0 (Immunoglobulin Fc Fragments)
0 (Immunoglobulin G)
0 (Receptors, IgG)

Date Created: 20140722 Date Completed: 20141007 Latest Revision: 20221109

20231215

PMC7430760

10.1038/ni.2939

25045879