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  • Title: Dominant suppression of inflammation by glycan-hydrolyzed IgG.
    Author: Nandakumar KS, Collin M, Happonen KE, Croxford AM, Lundström SL, Zubarev RA, Rowley MJ, Blom AM, Holmdahl R.
    Journal: Proc Natl Acad Sci U S A; 2013 Jun 18; 110(25):10252-7. PubMed ID: 23671108.
    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.
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