The carbohydrate switch between pathogenic and immunosuppressive antigen-specific antibodies.
Collin, Mattias LU
and Ehlers, Marc
(2013)
In Experimental Dermatology
22(8).
p.511-514
- Abstract
- IgG antibodies have one conserved N-glycosylation site at Asn 297 in each of their constant heavy chain regions. These Fc glycans influence the overall structure and pro- or anti-inflammatory effector functions of IgG antibodies. The biantennary core glycan structure, consisting of four N-acetyl-glucosamine (GlcNAc) and three mannose residues, can be further decorated with fucose, a bisecting GlcNAc and terminal galactose or galactose plus sialic acid. Non-galactosylated (agalactosylated; G0) IgG antibodies have long been associated with pro-inflammatory effector functions in autoimmune patients with rheumatoid arthritis (RA). In contrast, it has been shown that sialylated IgGs are responsible for anti-inflammatory effects of intravenous... (More)
- IgG antibodies have one conserved N-glycosylation site at Asn 297 in each of their constant heavy chain regions. These Fc glycans influence the overall structure and pro- or anti-inflammatory effector functions of IgG antibodies. The biantennary core glycan structure, consisting of four N-acetyl-glucosamine (GlcNAc) and three mannose residues, can be further decorated with fucose, a bisecting GlcNAc and terminal galactose or galactose plus sialic acid. Non-galactosylated (agalactosylated; G0) IgG antibodies have long been associated with pro-inflammatory effector functions in autoimmune patients with rheumatoid arthritis (RA). In contrast, it has been shown that sialylated IgGs are responsible for anti-inflammatory effects of intravenous immunoglobulin (IVIG; purified IgG from pooled human plasma), which is administered at high doses (2 g/kg) for the systemic treatment of autoimmune patients. It has become increasingly evident that pro-inflammatory immune responses, such as autoimmune reactions, primarily induce antigen-specific G0 IgGs, whereas tolerance induces immunosuppressive galactosylated and sialylated IgGs. Under physiological conditions, differentially glycosylated IgGs mediate their pro- or anti-inflammatory effector functions obviously as immune complexes (IC) in an antigen-specific manner. Therefore, antigen-specific galactosylated and sialylated IgGs may be a promising therapeutic tool for re-establishing tolerance against defined (self-) antigens in autoimmune or allergic patients. Here, we summarize these findings and outline our viewpoint on the development and function of differentially glycosylated antigen-specific IgG antibodies. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3956358
- author
- Collin, Mattias
LU
and Ehlers, Marc
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Experimental Dermatology
- volume
- 22
- issue
- 8
- pages
- 511 - 514
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000322158300002
- pmid:23808883
- scopus:84880708189
- pmid:23808883
- ISSN
- 0906-6705
- DOI
- 10.1111/exd.12171
- language
- English
- LU publication?
- yes
- id
- 4b752766-c46f-4683-999d-95e823eed703 (old id 3956358)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/23808883?dopt=Abstract
- date added to LUP
- 2016-04-01 09:49:31
- date last changed
- 2022-04-19 19:57:02
@article{4b752766-c46f-4683-999d-95e823eed703,
abstract = {{IgG antibodies have one conserved N-glycosylation site at Asn 297 in each of their constant heavy chain regions. These Fc glycans influence the overall structure and pro- or anti-inflammatory effector functions of IgG antibodies. The biantennary core glycan structure, consisting of four N-acetyl-glucosamine (GlcNAc) and three mannose residues, can be further decorated with fucose, a bisecting GlcNAc and terminal galactose or galactose plus sialic acid. Non-galactosylated (agalactosylated; G0) IgG antibodies have long been associated with pro-inflammatory effector functions in autoimmune patients with rheumatoid arthritis (RA). In contrast, it has been shown that sialylated IgGs are responsible for anti-inflammatory effects of intravenous immunoglobulin (IVIG; purified IgG from pooled human plasma), which is administered at high doses (2 g/kg) for the systemic treatment of autoimmune patients. It has become increasingly evident that pro-inflammatory immune responses, such as autoimmune reactions, primarily induce antigen-specific G0 IgGs, whereas tolerance induces immunosuppressive galactosylated and sialylated IgGs. Under physiological conditions, differentially glycosylated IgGs mediate their pro- or anti-inflammatory effector functions obviously as immune complexes (IC) in an antigen-specific manner. Therefore, antigen-specific galactosylated and sialylated IgGs may be a promising therapeutic tool for re-establishing tolerance against defined (self-) antigens in autoimmune or allergic patients. Here, we summarize these findings and outline our viewpoint on the development and function of differentially glycosylated antigen-specific IgG antibodies.}},
author = {{Collin, Mattias and Ehlers, Marc}},
issn = {{0906-6705}},
language = {{eng}},
number = {{8}},
pages = {{511--514}},
publisher = {{Wiley-Blackwell}},
series = {{Experimental Dermatology}},
title = {{The carbohydrate switch between pathogenic and immunosuppressive antigen-specific antibodies.}},
url = {{http://dx.doi.org/10.1111/exd.12171}},
doi = {{10.1111/exd.12171}},
volume = {{22}},
year = {{2013}},
}