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

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Bibtex

@article{9961a15bc3064da8a84f047ef6846fdd,
title = "Identification of the minimal glycopeptide core recognized by T cells in a model for rheumatoid arthritis",
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.",
keywords = "T cell, glycopeptide, collagen, rheumatoid arthritis",
author = "L Holm and P Kjellen and Rikard Holmdahl and J Kihlberg",
note = "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)",
year = "2005",
doi = "10.1016/j.bmc.2004.10.011",
language = "English",
volume = "13",
pages = "473--482",
journal = "Bioorganic and Medicinal Chemistry",
issn = "0968-0896",
publisher = "Elsevier",
number = "2",

}