Document Type

Article

Publication Date

1-1-2020

Abstract

EDITORIAL published: 07 August 2020 doi: 10.3389/fimmu.2020.01761 Frontiers in Immunology | www.frontiersin.org 1 August 2020 | Volume 11 | Article 1761 Edited by: Deborah K. Dunn-Walters, University of Surrey, United Kingdom Reviewed by: Roberta Pelanda, University of Colorado School of Medicine, United States *Correspondence: Sylvie Hermouet sylvie.hermouet@univ-nantes.fr Specialty section: This article was submitted to B Cell Biology, a section of the journal Frontiers in Immunology Received: 29 May 2020 Accepted: 30 June 2020 Published: 07 August 2020 Citation: Harb J, Wilson BS and Hermouet S (2020) Editorial: Structure, Isotypes, Targets, and Post-translational Modifications of Immunoglobulins and Their Role in Infection, Inflammation and Autoimmunity. Front. Immunol. 11:1761. doi: 10.3389/fimmu.2020.01761 Editorial: Structure, Isotypes, Targets, and Post-translational Modifications of Immunoglobulins and Their Role in Infection, Inflammation and Autoimmunity Jean Harb 1,2,3, Bridget S. Wilson 4,5 and Sylvie Hermouet 2,6* 1 Centre de Recherche en Transplantation et Immunologie UMR1064, Inserm, Université de Nantes, Nantes, France, 2 CRCINA, Inserm, Université de Nantes, Université d’Angers, Nantes, France, 3 Laboratoire de Biochimie, CHU de Nantes, Nantes, France, 4 University of New Mexico Comprehensive Cancer Center, Albuquerque, NM, United States, 5 Department of Pathology, University of New Mexico School of Medicine, Albuquerque, NM, United States, 6 Laboratoire d’Hématologie, CHU de Nantes, Nantes, France Keywords: immunoglobulins, glycosylation, targets, inflammation, infection, autoimmunity Editorial on the Research Topic Structure, Isotypes, Targets, and Post-translational Modifications of Immunoglobulins and Their Role in Infection, Inflammation and Autoimmunity Infection, autoimmunity, and cancer are accompanied by inflammation, which may alter the structure and function of immunoglobulins (Ig) and consequently, their pathogenicity (1–3). In addition, the isotype also influences the pathogenicity of Igs (4). During Dengue virus infection, the removal of core fucose residues selectively enhances the affinity of IgG for Fragment crystallizable (Fc)γIIIa receptors, leading to increased antibody-dependent cell mediated cytotoxicity (ADCC) and decreased complement dependent cytotoxicity (CDC) (5). In patients infected by the human immunodeficiency virus (HIV), anti-gp120 antibodies are less galactosylated and sialylated in asymptomatic, long-term non-progressors, compared to symptomatic patients (6). The Fc domain of IgGs can trigger pro- or anti-inflammatory responses and there is abundant evidence that carbohydrates attached to the IgG Fc domain are essential for IgG function (7–9). The pro- or anti-inflammatory function of IgGs is mediated by different affinities for activating FcγRs (FcγRI, RIIa, RIIIa, and RIIIb) and inhibiting FcγRIIb expressed by immune cells (10–12). A high level of sialylation of the IgG Fc fragment decreases ADCC potential through low affinity for activating receptors and conversely, bisecting N-acetylglucosamines on the Fc fragment are pro-inflammatory and enhance ADCC (13–16). In autoimmune diseases, such as rheumatoid arthritis, patients show low levels of IgG Fc sialylation, while increased IgG sialylation is associated with remission (17, 18). Thus, the glycosylation level of IgGs may explains their “protective” action. Similarly, Ig glycosylation plays an important role in IgA nephropathy, where IgA1s are deficient in galactose and not correctly cleared by anti-IgA1 antibodies (19)

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