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National Academy of Sciences, Proceedings of the National Academy of Sciences, 25(110), p. 10252-10257, 2013

DOI: 10.1073/pnas.1301480110

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Dominant suppression of inflammation by glycan hydrolyzed IgG

Journal article published in 2013 by Kutty Selva Nandakumar ORCID, Mattias Collin, Kaisa E. Happonen ORCID, Allyson M. Croxford, Susanna L. Lundström, Roman A. Zubarev, Merrill J. Rowley, Anna M. Blom, Rikard Holmdahl
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.