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Dominant suppression of inflammation by glycan-hydrolyzed IgG [Retracted]

På svenska

Author

  • Kutty Selva Nandakumar
  • Mattias Collin
  • Kaisa Happonen
  • Allyson M. Croxford
  • Susanna L. Lundstrom
  • Roman A. Zubarev
  • Merrill J. Rowley
  • Anna Blom
  • Rikard Holmdahl

Summary, in English

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.

Publishing year

2013

Language

English

Pages

10252-10257

Publication/Series

Proceedings of the National Academy of Sciences

Volume

110

Issue

25

Document type

Journal article

Publisher

National Academy of Sciences

Topic

  • Other Basic Medicine
  • Infectious Medicine

Keywords

  • collagen
  • endoglycosidase
  • glycosylation
  • monoclonal antibody
  • rheumatoid arthritis

Status

Published

Research group

  • Protein Chemistry, Malmö

ISBN/ISSN/Other

  • ISSN: 1091-6490