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

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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-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.

Detaljer

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

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Annan medicinsk grundvetenskap
  • Infektionsmedicin

Nyckelord

Originalspråkengelska
Sidor (från-till)10252-10257
TidskriftProceedings of the National Academy of Sciences
Volym110
Utgivningsnummer25
StatusPublished - 2013
PublikationskategoriForskning
Peer review utfördJa