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Endoglycosidase treatment abrogates IgG arthritogenicity: Importance of IgG glycosylation in arthritis.

Kutty Selva, Nandakumar LU ; Collin, Mattias LU ; Olsén, Arne LU ; Nimmerjahn, Falk ; Blom, Anna LU ; Ravetch, Jeffrey V and Holmdahl, Rikard LU (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)
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author
; ; ; ; ; and
organization
publishing date
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 and Sons
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
2021-01-06 02:57:09
@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},
  language     = {eng},
  number       = {10},
  pages        = {2973--2982},
  publisher    = {John Wiley and Sons},
  series       = {European Journal of Immunology},
  title        = {Endoglycosidase treatment abrogates IgG arthritogenicity: Importance of IgG glycosylation in arthritis.},
  url          = {https://lup.lub.lu.se/search/ws/files/2866122/626127.pdf},
  doi          = {10.1002/eji.200737581},
  volume       = {37},
  year         = {2007},
}