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Sialylation as an Important Regulator of Antibody Function

Antibodies play a critical role in linking the adaptive immune response to the innate immune system. In humans, antibodies are categorized into five classes, IgG, IgM, IgA, IgE, and IgD, based on constant region sequence, structure, and tropism. In serum, IgG is the most abundant antibody, comprisin...

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Autores principales: Vattepu, Ravi, Sneed, Sunny Lyn, Anthony, Robert M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9021442/
https://www.ncbi.nlm.nih.gov/pubmed/35464485
http://dx.doi.org/10.3389/fimmu.2022.818736
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author Vattepu, Ravi
Sneed, Sunny Lyn
Anthony, Robert M.
author_facet Vattepu, Ravi
Sneed, Sunny Lyn
Anthony, Robert M.
author_sort Vattepu, Ravi
collection PubMed
description Antibodies play a critical role in linking the adaptive immune response to the innate immune system. In humans, antibodies are categorized into five classes, IgG, IgM, IgA, IgE, and IgD, based on constant region sequence, structure, and tropism. In serum, IgG is the most abundant antibody, comprising 75% of antibodies in circulation, followed by IgA at 15%, IgM at 10%, and IgD and IgE are the least abundant. All human antibody classes are post-translationally modified by sugars. The resulting glycans take on many divergent structures and can be attached in an N-linked or O-linked manner, and are distinct by antibody class, and by position on each antibody. Many of these glycan structures on antibodies are capped by sialic acid. It is well established that the composition of the N-linked glycans on IgG exert a profound influence on its effector functions. However, recent studies have described the influence of glycans, particularly sialic acid for other antibody classes. Here, we discuss the role of glycosylation, with a focus on terminal sialylation, in the biology and function across all antibody classes. Sialylation has been shown to influence not only IgG, but IgE, IgM, and IgA biology, making it an important and unappreciated regulator of antibody function.
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spelling pubmed-90214422022-04-22 Sialylation as an Important Regulator of Antibody Function Vattepu, Ravi Sneed, Sunny Lyn Anthony, Robert M. Front Immunol Immunology Antibodies play a critical role in linking the adaptive immune response to the innate immune system. In humans, antibodies are categorized into five classes, IgG, IgM, IgA, IgE, and IgD, based on constant region sequence, structure, and tropism. In serum, IgG is the most abundant antibody, comprising 75% of antibodies in circulation, followed by IgA at 15%, IgM at 10%, and IgD and IgE are the least abundant. All human antibody classes are post-translationally modified by sugars. The resulting glycans take on many divergent structures and can be attached in an N-linked or O-linked manner, and are distinct by antibody class, and by position on each antibody. Many of these glycan structures on antibodies are capped by sialic acid. It is well established that the composition of the N-linked glycans on IgG exert a profound influence on its effector functions. However, recent studies have described the influence of glycans, particularly sialic acid for other antibody classes. Here, we discuss the role of glycosylation, with a focus on terminal sialylation, in the biology and function across all antibody classes. Sialylation has been shown to influence not only IgG, but IgE, IgM, and IgA biology, making it an important and unappreciated regulator of antibody function. Frontiers Media S.A. 2022-04-07 /pmc/articles/PMC9021442/ /pubmed/35464485 http://dx.doi.org/10.3389/fimmu.2022.818736 Text en Copyright © 2022 Vattepu, Sneed and Anthony https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Immunology
Vattepu, Ravi
Sneed, Sunny Lyn
Anthony, Robert M.
Sialylation as an Important Regulator of Antibody Function
title Sialylation as an Important Regulator of Antibody Function
title_full Sialylation as an Important Regulator of Antibody Function
title_fullStr Sialylation as an Important Regulator of Antibody Function
title_full_unstemmed Sialylation as an Important Regulator of Antibody Function
title_short Sialylation as an Important Regulator of Antibody Function
title_sort sialylation as an important regulator of antibody function
topic Immunology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9021442/
https://www.ncbi.nlm.nih.gov/pubmed/35464485
http://dx.doi.org/10.3389/fimmu.2022.818736
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