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

Nandakumar, Kutty Selva; Collin, Mattias LU ; Happonen, Kaisa E. LU ; Lundström, Susanna L.; Croxford, Allyson M.; Xu, Bingze; Zubarev, Roman A.; Rowley, Merrill J.; Blom, Anna M. LU and Kjellman, Christian, et al. (2018) In Frontiers in Immunology 9.
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... (More)
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. (Less)
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Frontiers in Immunology
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9
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Frontiers Media S. A.
external identifiers
  • scopus:85050070345
DOI
10.3389/fimmu.2018.01623
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English
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yes
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d566f7f9-1e9a-4428-b644-676331c8a722
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2018-07-24 10:31:09
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2019-08-14 04:20:19
@article{d566f7f9-1e9a-4428-b644-676331c8a722,
  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.},
  articleno    = {1623},
  author       = {Nandakumar, Kutty Selva and Collin, Mattias and Happonen, Kaisa E. and Lundström, Susanna L. and Croxford, Allyson M. and Xu, Bingze and Zubarev, Roman A. and Rowley, Merrill J. and Blom, Anna M. and Kjellman, Christian and Holmdahl, Rikard},
  language     = {eng},
  month        = {07},
  publisher    = {Frontiers Media S. A.},
  series       = {Frontiers in Immunology},
  title        = {Streptococcal Endo-β-N-Acetylglucosaminidase Suppresses Antibody-Mediated Inflammation In Vivo},
  url          = {http://dx.doi.org/10.3389/fimmu.2018.01623},
  volume       = {9},
  year         = {2018},
}