Dominant suppression of inflammation by glycan-hydrolyzed IgG
| Autor: | Allyson M. Croxford, Kaisa E. Happonen, Merrill J. Rowley, Susanna L. Lundström, Roman A. Zubarev, Rikard Holmdahl, Kutty Selva Nandakumar, Anna M. Blom, Mattias Collin |
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| Rok vydání: | 2013 |
| Předmět: |
0303 health sciences
Glycan Antigen-Antibody Complex Multidisciplinary biology Arthritis medicine.disease Molecular biology Immune complex Immunoglobulin G In vitro 3. Good health 03 medical and health sciences 0302 clinical medicine Biochemistry In vivo biology.protein medicine Antibody 030304 developmental biology 030215 immunology |
| Zdroj: | Proceedings of the National Academy of Sciences Proceedings of the National Academy of Sciences; Vol 110 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.1301480110 |
| Popis: | A unique anti-inflammatory property of IgG, independent of antigen specificity, is described. IgG with modification of the heavy-chain glycan on asparagine 297 by the streptococcal enzyme endo-β- N -acetylglucosaminidase (EndoS) induced a dominant suppression of immune complex (IC)-mediated inflammation, such as arthritis, through destabilization of local ICs by fragment crystallizable–fragment crystallizable (Fc-Fc) interactions. Small amounts (250 µg) of EndoS-hydrolyzed IgG were sufficient to inhibit arthritis in mice and most effective during the formation of ICs in the target tissue. The presence of EndoS-hydrolyzed IgG disrupted larger IC lattice formation both in vitro and in vivo, as visualized with anti-C3b staining. Neither complement binding in vitro nor antigen–antibody binding per se was affected. |
| Databáze: | OpenAIRE |
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