title: Sweet but dangerous - the role of immunoglobulin G glycosylation in autoimmunity and inflammation.
abstract: Glycosylation is well-known to modulate the functional capabilities of immunoglobulin G (IgG)-mediated cellular and humoral responses. Indeed, highly sialylated and desialylated IgG is endowed with anti- and pro-inflammatory activities, respectively, whereas fully deglycosylated IgG is a rather lame duck, with no effector function besides toxin neutralization. Recently, several studies revealed the impact of different glycosylation patterns on the Fc part and Fab fragment of IgG in several autoimmune diseases, including systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA). Here, we provide a synoptic update summarizing the most important aspects of antibody glycosylation, and the current progress in this field. We also discuss the therapeutic options generated by the modification of the glycosylation of IgG in a potential treatment for chronic inflammatory diseases.
authors.affiliation: Friedrich-Alexander-University Erlangen-Nürnberg (FAU), Department of Internal Medicine 3 - Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany.
authors.forename: M H C
authors.initials: MH
authors.lastname: Biermann
authors.affiliation: Friedrich-Alexander-University Erlangen-Nürnberg (FAU), Department of Internal Medicine 3 - Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany.
authors.forename: G
authors.initials: G
authors.lastname: Griffante
authors.affiliation: Friedrich-Alexander-University Erlangen-Nürnberg (FAU), Department of Internal Medicine 3 - Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany.
authors.forename: M J
authors.initials: MJ
authors.lastname: Podolska
authors.affiliation: Friedrich-Alexander-University Erlangen-Nürnberg (FAU), Department of Internal Medicine 3 - Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany.
authors.forename: S
authors.initials: S
authors.lastname: Boeltz
authors.affiliation: Friedrich-Alexander-University Erlangen-Nürnberg (FAU), Department of Internal Medicine 3 - Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Stürmer
authors.affiliation: Friedrich-Alexander-University Erlangen-Nürnberg (FAU), Department of Internal Medicine 3 - Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany.
authors.forename: L E
authors.initials: LE
authors.lastname: Muñoz
authors.affiliation: Friedrich-Alexander-University Erlangen-Nürnberg (FAU), Department of Internal Medicine 3 - Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany Danylo Halytsky Lviv National Medical University, Lviv, Ukraine.
authors.forename: R
authors.initials: R
authors.lastname: Bilyy
authors.affiliation: Friedrich-Alexander-University Erlangen-Nürnberg (FAU), Department of Internal Medicine 3 - Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany martin.herrmann@uk-erlangen.de.
authors.forename: M
authors.initials: M
authors.lastname: Herrmann
mesh_terms: D001172:Arthritis, Rheumatoid / Q000276:immunology*; D001323:Autoantibodies / Q000097:blood*; D006031:Glycosylation; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000276:immunology*; D007074:Immunoglobulin G / Q000276:immunology*; D008180:Lupus Erythematosus, Systemic / Q000276:immunology*; D006023:Glycoproteins
chemical_list: D001323:Autoantibodies; D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G; C046179:glycosylated IgG; D006023:Glycoproteins
keywords: Fc fragment; Glycosylation; autoantibody; autoimmunity; fucosylation; galactosylation; inflammation; sialylation