A Comparison of Immunoglobulin Variable Region N-Linked Glycosylation in Healthy Donors, Autoimmune Disease and Lymphoma.

Frontiers in Immunology
Esther M VletterRené E M Toes

Abstract

N-linked glycans play an important role in immunity. Although the role of N-linked glycans in the Fragment crystallizable (Fc) region of immunoglobulins has been thoroughly described, the function of N-linked glycans present in Ig-variable domains is only just being appreciated. Most of the N-linked glycans harbored by immunoglobulin variable domain are of the complex biantennary type and are found as a result of the presence of N-linked glycosylation that most often have been introduced by somatic hypermutation. Furthermore, these glycans are ubiquitously present on autoantibodies observed in some autoimmune diseases as well as certain B-cell lymphomas. For example, variable domain glycans are abundantly found by anti-citrullinated protein antibodies (ACPA) in rheumatoid arthritis (RA) as well as by the B-cell receptors of follicular lymphoma (FL). In FL, variable domain glycans are postulated to convey a selective advantage through interaction with lectins and/or microbiota, whereas the contribution of variable domain glycans on autoantibodies is not known. To aid the understanding how these seemingly comparable phenomena contribute to a variety of deranged B-responses in such different diseases this study summarizes the char...Continue Reading

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Citations

Sep 3, 2020·Cells·Anna IllianoAngela Amoresano
Jul 29, 2020·Viruses·Monika A ZelazowskaLaurie T Krug
Aug 6, 2020·International Journal of Molecular Sciences·Yuliya V MarkinaAlexander N Orekhov
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Feb 6, 2021·Analytical Methods : Advancing Methods and Applications·Huifei ZhongRui Zhao
Nov 3, 2021·Scandinavian Journal of Rheumatology·J KoersT Rispens

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Methods Mentioned

BETA
glycosylation
biopsies

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