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

Nandakumar, Kutty Selva; Collin, Mattias LU ; Happonen, Kaisa LU ; Croxford, Allyson M.; Lundstrom, Susanna L.; Zubarev, Roman A.; Rowley, Merrill J.; Blom, Anna LU and Holmdahl, Rikard (2013) In Proceedings of the National Academy of Sciences 110(25). p.10252-10257
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
collagen, endoglycosidase, glycosylation, monoclonal antibody, rheumatoid arthritis
in
Proceedings of the National Academy of Sciences
volume
110
issue
25
pages
10252 - 10257
publisher
National Acad Sciences
external identifiers
  • wos:000321500200054
  • scopus:84879310116
ISSN
1091-6490
DOI
10.1073/pnas.1301480110
language
English
LU publication?
yes
id
3b6c1b99-d9c9-4aa0-b7e0-f69a991a5500 (old id 4039645)
date added to LUP
2013-10-01 15:15:01
date last changed
2019-06-25 01:09:38
@article{3b6c1b99-d9c9-4aa0-b7e0-f69a991a5500,
  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.},
  author       = {Nandakumar, Kutty Selva and Collin, Mattias and Happonen, Kaisa and Croxford, Allyson M. and Lundstrom, Susanna L. and Zubarev, Roman A. and Rowley, Merrill J. and Blom, Anna and Holmdahl, Rikard},
  issn         = {1091-6490},
  keyword      = {collagen,endoglycosidase,glycosylation,monoclonal antibody,rheumatoid arthritis},
  language     = {eng},
  number       = {25},
  pages        = {10252--10257},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {Dominant suppression of inflammation by glycan-hydrolyzed IgG [Retracted]},
  url          = {http://dx.doi.org/10.1073/pnas.1301480110},
  volume       = {110},
  year         = {2013},
}