Cartilage-specific autoimmunity in rheumatoid arthritis: characterization of a triple helical B cell epitope in the integrin-binding-domain of collagen type II.

Abstract:

:Cartilage-specific proteins are considered potential autoantigens that could continuously fuel autoimmune responses directed to the joints in rheumatoid arthritis (RA). Using recombinant chimeric collagen type II we have identified one major type II collagen (CII) epitope (denoted U1) recognized by RA sera. The U1 epitope is a triple helical structure formed by 11 amino acids (triple helical position 494-504) and colocalizes with the recently described alpha1beta1/alpha2beta1 integrin binding site. It is a major epitope, found in 14/22 RA sera positive for antibodies to CII. One individual could be followed for a long time and the results showed that IgG antibodies specific for the U1 epitope were maintained along the chronic disease course but suppressed during periods of cyclosporin A and anti-CD4 treatment. We also found that the U1 epitope was recognized in rats susceptible to collagen-induced arthritis. A monoclonal autoantibody (mAb 126.30) was raised from DA rats, which bound the same epitope. The antibodies bound the cartilage in vivo showing that the epitope is exposed to the immune system for immune complex formation in the intact joint.

journal_name

Eur J Immunol

authors

Kraetsch HG,Unger C,Wernhoff P,Schneider C,Kalden JR,Holmdahl R,Burkhardt H

doi

10.1002/1521-4141(200106)31:6<1666::aid-immu1666>3

keywords:

subject

Has Abstract

pub_date

2001-06-01 00:00:00

pages

1666-73

issue

6

eissn

0014-2980

issn

1521-4141

pii

10.1002/1521-4141(200106)31:6<1666::AID-IMMU1666>3

journal_volume

31

pub_type

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