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Literature DB >> 30805712

IgG Fc Glycosylation in Human Immunity.

Abstract

Glycosylation of IgG Fc domains is a central mechanism in the diversification of antibody function. Modifications to the core Fc glycan impact antibody function by shifting the balance of Type I and Type II Fc gamma receptors (FcγR) that will be engaged by immune complexes. This, in turn, modulates the effector cells and functions that can be recruited during immune activation. Critically, humans have evolved to regulate Fc glycan modifications for immune homeostasis. Dysregulation in Fc glycan modifications can lead to loss of immune tolerance, symptomatic autoimmunity, and susceptibility to infectious diseases. Here, we discuss IgG Fc glycosylation and its role in human health and disease.

Entities: Chemical Disease Gene Mutation Species

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Year: 2019 PMID： 30805712 PMCID： PMC7853246 DOI： 10.1007/82_2019_152

Source DB: PubMed Journal: Curr Top Microbiol Immunol ISSN： 0070-217X Impact factor: 4.291

65 in total

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3. Clinical characteristics and outcomes of patients with severe covid-19 with diabetes.

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Journal: BMJ Open Diabetes Res Care Date: 2020-04

Review 4. SARS-CoV-2 vaccines in advanced clinical trials: Where do we stand?

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Journal: Nat Immunol Date: 2020-11-09 Impact factor: 25.606

7. Changes of IgG N-Glycosylation in Thyroid Autoimmunity: The Modulatory Effect of Methimazole in Graves' Disease and the Association With the Severity of Inflammation in Hashimoto's Thyroiditis.

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Review 9. Role of Immunoglobulins in Muscular Dystrophies and Inflammatory Myopathies.

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10. Early non-neutralizing, afucosylated antibody responses are associated with COVID-19 severity.

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