Streptococcal Endo-β-N-Acetylglucosaminidase Suppresses Antibody-Mediated Inflammation In Vivo

Kutty Selva Nandakumar, Mattias Collin, Kaisa E. Happonen, Susanna L. Lundström, Allyson M. Croxford, Bingze Xu, Roman A. Zubarev, Merrill J. Rowley, Anna M. Blom, Christian Kjellman, Rikard Holmdahl

Research output: Contribution to journalArticlepeer-review

9 Citations (SciVal)

Abstract

Endo-β-N-acetylglucosaminidase (EndoS) is a family 18 glycosyl hydrolase secreted by Streptococcus pyogenes. Recombinant EndoS hydrolyzes the β-1,4-di-N-acetylchitobiose core of the N-linked complex type glycan on the asparagine 297 of the γ-chains of IgG. Here, we report that EndoS and IgG hydrolyzed by EndoS induced suppression of local immune complex (IC)-mediated arthritis. A small amount (1 µg given i.v. to a mouse) of EndoS was sufficient to inhibit IgG-mediated arthritis in mice. The presence of EndoS disturbed 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 were affected. Thus, EndoS could potentially be used for treating patients with IC-mediated pathology.
Original languageEnglish
Article number1623
JournalFrontiers in Immunology
Volume9
DOIs
Publication statusPublished - 2018 Jul 16

Subject classification (UKÄ)

  • Immunology in the medical area

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