Dominant suppression of inflammation by glycan-hydrolyzed IgG [Retracted]
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4039645
- author
- 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
- organization
- publishing date
- 2013
- 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 Academy of Sciences
- external identifiers
-
- wos:000321500200054
- scopus:84879310116
- pmid:23671108
- ISSN
- 1091-6490
- DOI
- 10.1073/pnas.1301480110
- language
- English
- LU publication?
- yes
- additional info
- This article has been retracted. Please see retraction note at:http://www.pnas.org/content/111/44/15851.1.full
- id
- 3b6c1b99-d9c9-4aa0-b7e0-f69a991a5500 (old id 4039645)
- date added to LUP
- 2016-04-01 10:14:14
- date last changed
- 2022-05-05 20:04:47
@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}}, keywords = {{collagen; endoglycosidase; glycosylation; monoclonal antibody; rheumatoid arthritis}}, language = {{eng}}, number = {{25}}, pages = {{10252--10257}}, publisher = {{National Academy of 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}}, doi = {{10.1073/pnas.1301480110}}, volume = {{110}}, year = {{2013}}, }