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The history of IgG glycosylation and where we are now.

ABSTRACT: IgG glycosylation is currently at the forefront of both immunology and glycobiology, likely due in part to the widespread and growing use of antibodies as drugs. For over four decades, it has been recognized that the conserved N-linked glycan on asparagine 297 found within the second Ig domain of the heavy chain (CH2) that helps to comprise Fc region of IgG plays a special role in IgG structure and function. Changes in galactosylation, fucosylation and sialylation are now well-established factors, which drive differential IgG function, ranging from inhibitory/anti-inflammatory to activating complement and promoting antibody-dependent cellular cytotoxicity. Thus, if we are to truly understand how to design and deploy antibody-based drugs with maximal efficacy and evaluate proper vaccine responses from a protective and functional perspective, a deep understanding of IgG glycosylation is essential. This article is intended to provide a comprehensive review of the IgG glycosylation field and the impact glycans have on IgG function, beginning with the earliest findings over 40 years ago, in order to provide a robust foundation for moving forward.

SUBMITTER: Cobb BA

PROVIDER: S-EPMC7109348 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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The history of IgG glycosylation and where we are now.

Cobb Brian A BA

Glycobiology 20200301 4

IgG glycosylation is currently at the forefront of both immunology and glycobiology, likely due in part to the widespread and growing use of antibodies as drugs. For over four decades, it has been recognized that the conserved N-linked glycan on asparagine 297 found within the second Ig domain of the heavy chain (CH2) that helps to comprise Fc region of IgG plays a special role in IgG structure and function. Changes in galactosylation, fucosylation and sialylation are now well-established factor ...[more]

PMID: 31504525

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Project description:BackgroundInflammation plays a key role in the progression of atherosclerotic plaque for peripheral artery disease (PAD). Immunoglobulin G (IgG) glycosylation could modulate immunological effector functions and has been explored as biomarkers for various diseases.MethodsLectin microarray was applied to analyze the expression profile of serum IgG glycosylation in patients with lower-extremity peripheral artery disease (LEPAD), carotid artery stenosis (CAS), abdominal aortic aneurysm (AAA), and healthy controls. Lectin blot was performed to validate the differences.ResultsSNA (Sambucus nigra agglutinin) binding (preferred sialic acid) was significantly higher in the LEPAD (3.21 ± 2.06) and AAA (3.34 ± 2.42) groups compared to the CAS (2.47 ± 1.45) group. Significantly higher binding levels of ConA (Concanavalin A) (preferred mannose) and PSA (Pisum sativum agglutinin) (preferred fucose) were also observed in LEPAD compared to CAS patients. Among LEPAD patients, a significant lower binding level of Black bean crude (preferred GalNAc) was present for dyslipidemia patients. A higher binding level of MNA-M (Morniga M agglutinin) (preferred Mannose) and Jacalin-AIA (Artocarpus integrifolia agglutinin) (preferred Galβ3GalNAc) was observed for Fontaine severe patients. Higher binding levels of PHA-E (Phaseolus vulgaris Erythroagglutinin) and PHA-L (Phaseolus vulgaris Leucoagglutinin) (preferred Galβ4GlcNAc) were observed for diabetic patients, and higher binding of ASA (Allium sativum agglutinin) (preferred Mannose) was present in patients with hypertension. The level of high-sensitivity C-reactive protein (hsCRP) was positively associated with LTL (Lotus tetragonolobus lectin) (r = 0.44), PSA (r = 0.44), LCA (Lens Culinaris agglutinin) (r = 0.39), SNA (r = 0.57), and CSA (Cytisus sscoparius agglutinin) (r = 0.56). For CAS, symptomatic patients had lower binding levels of AAL (Aleuria aurantia lectin) (preferred fucose) and IAA (Iberis amara agglutinin) (preferred GalNAc). Blood total cholesterol level was positively associated with SNA-I (r = 0.36) and SBA (Soybean agglutinin) (r = r = 0.35). Creatinine levels were positively associated with lectins including, but not limited to, MNA-M (r = 0.42), CSA (r = 0.45), GHA (Glechoma hederacea agglutinin) (r = 0.42), and MNA-G (Morniga G agglutinin) (r = 0.45).ConclusionLEPAD patients had increased IgG binding levels of SNA and ConA compared to CAS, which could provide potential diagnostic value. Fontaine severity was associated with Mannose-rich IgG N-glycan, while diabetic LEPAD correlated with bisecting GlcNAc. The levels of hsCRP and creatinine were positively associated with IgG fucosylation and galactosylation. Changes in IgG glycosylation may play important roles in PAD pathogenesis and progression.

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The history of IgG glycosylation and where we are now.

Publications

The history of IgG glycosylation and where we are now.

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