IgG-effector functions: “The Good, The Bad and The Ugly”

• Published in: Immunology letters Vol. 160; no. 2; pp. 139 - 144
• Main Authors: Kapur, Rick, Einarsdottir, Helga K, Vidarsson, Gestur
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-08-2014
• Subjects: Allergy and Immunology; Autoimmune Diseases - metabolism; Autoimmune Diseases - pathology; Communicable Diseases - immunology; Communicable Diseases - metabolism; Communicable Diseases - pathology; Complement System Proteins - genetics; Complement System Proteins - metabolism; FcgR polymorphism; Female; Gene Expression Regulation - immunology; Glycosylation; Humans; IgG allotypes; IgG glycosylation; Immunity, Humoral; Immunoglobulin G - genetics; Immunoglobulin G - immunology; Immunoglobulin G - metabolism; Models, Molecular; Placenta - immunology; Placenta - metabolism; Polymorphism, Genetic; Pregnancy; Protein Binding; Protein Processing, Post-Translational; Receptors, IgG - genetics; Receptors, IgG - immunology; Receptors, IgG - metabolism; IgG allotypes; IgG glycosylation; FcgR polymorphism
• ISSN: 0165-2478; 1879-0542
• DOI: 10.1016/j.imlet.2014.01.015

Highlights • FcγR polymorphisms affect binding to IgG and thereby strength of immune reactions. • Likewise, FcγR-IgG binding is affected by which IgG subclasses are involved. • Biological differences between IgG allotypes also exist, particularly for IgG3. • IgG effector functions are also strongly affected by IgG-Fc glycosylation patterns. • IgG-Fc glycan type is antigen dependent, ultimately governed on the B-cell level.