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Identification of the minimal glycopeptide core recognized by T cells in a model for rheumatoid arthritis

Holm, L; Kjellen, P; Holmdahl, Rikard LU and Kihlberg, J (2005) In Bioorganic & Medicinal Chemistry 13(2). p.473-482
Abstract
Collagen induced arthritis (CIA) is a common mouse model for rheumatoid arthritis. Two sets of truncated peptides derived from type II collagen have been prepared and tested for binding to A(q), a MHC-II molecule associated with development of CIA. Binding to A(q) correlated well with predictions from a computer-based model. T-cell hybridomas, obtained in CIA, were also used to study the ability of A(q) bound peptides to trigger a T-cell response. The minimal peptide epitope required for binding, as well as for giving a T-cell response, was determined to be CII260-267. In collagen this epitope is often glycosylated at hydroxylysine 264 and glycosylation has been shown to be an immunodominant feature in CIA. Synthesis and evaluation of... (More)
Collagen induced arthritis (CIA) is a common mouse model for rheumatoid arthritis. Two sets of truncated peptides derived from type II collagen have been prepared and tested for binding to A(q), a MHC-II molecule associated with development of CIA. Binding to A(q) correlated well with predictions from a computer-based model. T-cell hybridomas, obtained in CIA, were also used to study the ability of A(q) bound peptides to trigger a T-cell response. The minimal peptide epitope required for binding, as well as for giving a T-cell response, was determined to be CII260-267. In collagen this epitope is often glycosylated at hydroxylysine 264 and glycosylation has been shown to be an immunodominant feature in CIA. Synthesis and evaluation of CII260-267 carrying a beta-D-galactosyl moiety at position 264 revealed that this glycopeptide stimulated representative members from a panel of carbohydrate-specific T-cell hybridomas obtained in CIA. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
T cell, glycopeptide, collagen, rheumatoid arthritis
in
Bioorganic & Medicinal Chemistry
volume
13
issue
2
pages
473 - 482
publisher
Elsevier
external identifiers
  • pmid:15598569
  • wos:000226343800018
  • scopus:10444240315
ISSN
0968-0896
DOI
10.1016/j.bmc.2004.10.011
language
English
LU publication?
yes
id
9961a15b-c306-4da8-a84f-047ef6846fdd (old id 257653)
date added to LUP
2007-08-15 11:01:20
date last changed
2017-01-01 04:42:19
@article{9961a15b-c306-4da8-a84f-047ef6846fdd,
  abstract     = {Collagen induced arthritis (CIA) is a common mouse model for rheumatoid arthritis. Two sets of truncated peptides derived from type II collagen have been prepared and tested for binding to A(q), a MHC-II molecule associated with development of CIA. Binding to A(q) correlated well with predictions from a computer-based model. T-cell hybridomas, obtained in CIA, were also used to study the ability of A(q) bound peptides to trigger a T-cell response. The minimal peptide epitope required for binding, as well as for giving a T-cell response, was determined to be CII260-267. In collagen this epitope is often glycosylated at hydroxylysine 264 and glycosylation has been shown to be an immunodominant feature in CIA. Synthesis and evaluation of CII260-267 carrying a beta-D-galactosyl moiety at position 264 revealed that this glycopeptide stimulated representative members from a panel of carbohydrate-specific T-cell hybridomas obtained in CIA.},
  author       = {Holm, L and Kjellen, P and Holmdahl, Rikard and Kihlberg, J},
  issn         = {0968-0896},
  keyword      = {T cell,glycopeptide,collagen,rheumatoid arthritis},
  language     = {eng},
  number       = {2},
  pages        = {473--482},
  publisher    = {Elsevier},
  series       = {Bioorganic & Medicinal Chemistry},
  title        = {Identification of the minimal glycopeptide core recognized by T cells in a model for rheumatoid arthritis},
  url          = {http://dx.doi.org/10.1016/j.bmc.2004.10.011},
  volume       = {13},
  year         = {2005},
}