Sudo, Makoto; Yamaguchi, Yoshiki; Späth, Peter Julius; Matsumoto-Morita, Kana; Ong, Benjamin K.; Shahrizaila, Nortina; Yuki, Nobuhiro (2014). Different IVIG glycoforms affect in vitro inhibition of anti-ganglioside antibody-mediated complement deposition. PLoS ONE, 9(9), e107772. Public Library of Science 10.1371/journal.pone.0107772
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Intravenous immunoglobulin (IVIG) is the first line treatment for Guillain–Barré syndrome and multifocal motor neuropathy, which are caused by anti-ganglioside antibody-mediated complement-dependent cytotoxicity. IVIG has many potential mechanisms of action, and sialylation of the IgG Fc portion reportedly has an anti-inflammatory effect in antibody-dependent cell-mediated cytotoxicity models. We investigated the effects of different IVIG glycoforms on the inhibition of antibody-mediated complement-dependent cytotoxicity. Deglycosylated, degalactosylated, galactosylated and sialylated IgG were prepared from IVIG following treatment with glycosidases and glycosyltransferases. Sera from patients with Guillain–Barré syndrome, Miller Fisher syndrome and multifocal motor neuropathy associated with anti-ganglioside antibodies were used. Inhibition of complement deposition subsequent to IgG or IgM autoantibody binding to ganglioside, GM1 or GQ1b was assessed on microtiter plates. Sialylated and galactosylated IVIGs more effectively inhibited C3 deposition than original IVIG or enzyme-treated IVIGs (agalactosylated and deglycosylated IVIGs). Therefore, sialylated and galactosylated IVIGs may be more effective than conventional IVIG in the treatment of complement-dependent autoimmune diseases.
Item Type: |
Journal Article (Original Article) |
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Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Pharmacology |
UniBE Contributor: |
Späth, Peter Julius |
Subjects: |
600 Technology > 610 Medicine & health |
ISSN: |
1932-6203 |
Publisher: |
Public Library of Science |
Language: |
English |
Submitter: |
Anita Dähler |
Date Deposited: |
19 Jan 2015 11:37 |
Last Modified: |
05 Dec 2022 14:39 |
Publisher DOI: |
10.1371/journal.pone.0107772 |
PubMed ID: |
25259950 |
BORIS DOI: |
10.7892/boris.61965 |
URI: |
https://boris.unibe.ch/id/eprint/61965 |