Endoglycosidase treatment abrogates IgG arthritogenicity: Importance of IgG glycosylation in arthritis.
(2007) In European Journal of Immunology 37(10). p.2973-2982- Abstract
- The glycosylation status of IgG has been implicated in the pathology of rheumatoid arthritis. Earlier, we reported the identification of a novel secreted endo-beta-N-acetylglucosaminidase (EndoS), secreted by Streptococcus pyogenes that specifically hydrolyzes the beta-1,4-di-N-acetylchitobiose core of the asparagine-linked glycan of human IgG. Here, we analyzed the arthritogenicity of EndoS-treated collagen type II (CII) -specific mouse mAb in vivo. Endoglycosidase treatment of the antibodies inhibited the induction of arthritis in (BALB/c x B10.Q) F1 mice and induced a milder arthritis in B10.RIII mice as compared with the severe arthritis induced by non-treated antibodies. Furthermore, EndoS treatment did not affect the binding of IgG... (More)
- The glycosylation status of IgG has been implicated in the pathology of rheumatoid arthritis. Earlier, we reported the identification of a novel secreted endo-beta-N-acetylglucosaminidase (EndoS), secreted by Streptococcus pyogenes that specifically hydrolyzes the beta-1,4-di-N-acetylchitobiose core of the asparagine-linked glycan of human IgG. Here, we analyzed the arthritogenicity of EndoS-treated collagen type II (CII) -specific mouse mAb in vivo. Endoglycosidase treatment of the antibodies inhibited the induction of arthritis in (BALB/c x B10.Q) F1 mice and induced a milder arthritis in B10.RIII mice as compared with the severe arthritis induced by non-treated antibodies. Furthermore, EndoS treatment did not affect the binding of IgG to CII and their ability to activate complement, but it resulted in reduced IgG binding to Fc gamma R and disturbed the formation of stable immune complexes. Hence, the asparagine-linked glycan on IgG plays a crucial role in the development of arthritis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/607491
- author
- Kutty Selva, Nandakumar
LU
; Collin, Mattias
LU
; Olsén, Arne LU ; Nimmerjahn, Falk ; Blom, Anna LU
; Ravetch, Jeffrey V and Holmdahl, Rikard LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- IgG, arthritis, endoS
- in
- European Journal of Immunology
- volume
- 37
- issue
- 10
- pages
- 2973 - 2982
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000250294100031
- scopus:35348875440
- ISSN
- 1521-4141
- DOI
- 10.1002/eji.200737581
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Medical Inflammation Research (013212019), Division of Infection Medicine (BMC) (013024020), Department of Laboratory Medicine, Lund (013017000), Department of Experimental Medical Science (013210000), Protein Chemistry (013017510)
- id
- e4272048-29db-4f22-bbe6-bcb42696d912 (old id 607491)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17899548&dopt=Abstract
- date added to LUP
- 2016-04-01 12:17:58
- date last changed
- 2022-05-14 20:22:32
@article{e4272048-29db-4f22-bbe6-bcb42696d912, abstract = {{The glycosylation status of IgG has been implicated in the pathology of rheumatoid arthritis. Earlier, we reported the identification of a novel secreted endo-beta-N-acetylglucosaminidase (EndoS), secreted by Streptococcus pyogenes that specifically hydrolyzes the beta-1,4-di-N-acetylchitobiose core of the asparagine-linked glycan of human IgG. Here, we analyzed the arthritogenicity of EndoS-treated collagen type II (CII) -specific mouse mAb in vivo. Endoglycosidase treatment of the antibodies inhibited the induction of arthritis in (BALB/c x B10.Q) F1 mice and induced a milder arthritis in B10.RIII mice as compared with the severe arthritis induced by non-treated antibodies. Furthermore, EndoS treatment did not affect the binding of IgG to CII and their ability to activate complement, but it resulted in reduced IgG binding to Fc gamma R and disturbed the formation of stable immune complexes. Hence, the asparagine-linked glycan on IgG plays a crucial role in the development of arthritis.}}, author = {{Kutty Selva, Nandakumar and Collin, Mattias and Olsén, Arne and Nimmerjahn, Falk and Blom, Anna and Ravetch, Jeffrey V and Holmdahl, Rikard}}, issn = {{1521-4141}}, keywords = {{IgG; arthritis; endoS}}, language = {{eng}}, number = {{10}}, pages = {{2973--2982}}, publisher = {{John Wiley & Sons Inc.}}, series = {{European Journal of Immunology}}, title = {{Endoglycosidase treatment abrogates IgG arthritogenicity: Importance of IgG glycosylation in arthritis.}}, url = {{https://lup.lub.lu.se/search/files/2866122/626127.pdf}}, doi = {{10.1002/eji.200737581}}, volume = {{37}}, year = {{2007}}, }