期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 25, 页码 10252-10257出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1301480110
关键词
collagen; endoglycosidase; glycosylation; monoclonal antibody; rheumatoid arthritis
资金
- King Gustaf V:s 80 Years Foundation
- Swedish Rheumatism Association
- Ake Wiberg
- Swedish Society for Medicine
- Royal Physiografic Society in Lund
- Medical Faculty at Lund University
- Swedish governmental
- Swedish Research Council [2009-2338, 2010-57X-20240, K2012-66X-14928-09-5]
- European Union [HEALTH-F2-2008-223404]
- National Health and Medical Research Council of Australia
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-beta-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 mu g) 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.
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