Publications
2009
Schett G, Dumortier H, Hoefler E, Muller S, Steiner G
B cell epitopes of the heterogeneous nuclear ribonucleoprotein A2: identification of a new specific antibody marker for active lupus disease Article de journal
Dans: Annals of the Rheumatic Diseases, vol. 68, no. 5, p. 729–735, 2009, ISSN: 1468-2060.
Résumé | Liens | BibTeX | Étiquettes: Autoantibodies, B-Lymphocyte, Biomarkers, Dumortier, Enzyme-Linked Immunosorbent Assay, Epitopes, Female, Follow-Up Studies, Heterogeneous-Nuclear Ribonucleoprotein Group A-B, Humans, I2CT, Lupus Erythematosus, Male, Rheumatic Diseases, Severity of Illness Index, Systemic, Team-Dumortier
@article{schett_b_2009,
title = {B cell epitopes of the heterogeneous nuclear ribonucleoprotein A2: identification of a new specific antibody marker for active lupus disease},
author = {G Schett and H Dumortier and E Hoefler and S Muller and G Steiner},
doi = {10.1136/ard.2007.087502},
issn = {1468-2060},
year = {2009},
date = {2009-05-01},
journal = {Annals of the Rheumatic Diseases},
volume = {68},
number = {5},
pages = {729--735},
abstract = {OBJECTIVES: Autoantibody formation and T cell reactivity against the heterogeneous nuclear ribonucleoprotein A2 (hnRNP-A2) has been observed in patients with rheumatoid arthritis (RA) and systemic lupus erythematosus (SLE). Since no differences in epitope recognition were reported and the usefulness of anti-hnRNP-A2 antibodies as diagnostic markers of SLE is unknown, it was our objective to characterise linear B cell epitopes of hnRNP-A2 and to relate the anti-hnRNP-A2 antibody responses to disease activity and clinical features of SLE.
METHODS: Sequential serum samples from 15 patients with SLE and sera from patients with other rheumatic diseases and healthy subjects were investigated by ELISA for autoantibody reactivities against a set of 13 overlapping peptides spanning the RNA-binding region of hnRNP-A2. Antibody reactivity against the complete protein was determined by western immunoblotting and ELISA. SLE disease activity was assessed by European Consensus Lupus Activity Measure scores, by SLE Index scores and the British Isles Lupus Assessment index.
RESULTS: Anti-peptide antibody reactivities were found in 60% of SLE sera but in only 5% of control samples, and were mainly directed to four peptides, one of which (p155-175) appeared to be immunodominant. Antibodies to p155-175 were exclusively seen in patients with SLE and correlated with clinical disease activity as well as kidney and skin involvement. No correlations were found for the other anti-peptide antibody responses.
CONCLUSION: Peptide p155-175 encompasses a disease-specific immunodominant epitope of hnRNP-A2. Since antibodies to p155-175 correlate with disease activity and nephritis, they may be useful as markers for active SLE.},
keywords = {Autoantibodies, B-Lymphocyte, Biomarkers, Dumortier, Enzyme-Linked Immunosorbent Assay, Epitopes, Female, Follow-Up Studies, Heterogeneous-Nuclear Ribonucleoprotein Group A-B, Humans, I2CT, Lupus Erythematosus, Male, Rheumatic Diseases, Severity of Illness Index, Systemic, Team-Dumortier},
pubstate = {published},
tppubtype = {article}
}
METHODS: Sequential serum samples from 15 patients with SLE and sera from patients with other rheumatic diseases and healthy subjects were investigated by ELISA for autoantibody reactivities against a set of 13 overlapping peptides spanning the RNA-binding region of hnRNP-A2. Antibody reactivity against the complete protein was determined by western immunoblotting and ELISA. SLE disease activity was assessed by European Consensus Lupus Activity Measure scores, by SLE Index scores and the British Isles Lupus Assessment index.
RESULTS: Anti-peptide antibody reactivities were found in 60% of SLE sera but in only 5% of control samples, and were mainly directed to four peptides, one of which (p155-175) appeared to be immunodominant. Antibodies to p155-175 were exclusively seen in patients with SLE and correlated with clinical disease activity as well as kidney and skin involvement. No correlations were found for the other anti-peptide antibody responses.
CONCLUSION: Peptide p155-175 encompasses a disease-specific immunodominant epitope of hnRNP-A2. Since antibodies to p155-175 correlate with disease activity and nephritis, they may be useful as markers for active SLE.
1999
Dumortier H, Abbal M, Fort M, Briand J P, Cantagrel A, Muller S
MHC class II gene associations with autoantibodies to U1A and SmD1 proteins Article de journal
Dans: International Immunology, vol. 11, no. 2, p. 249–257, 1999, ISSN: 0953-8178.
Résumé | Liens | BibTeX | Étiquettes: Alleles, Antibody Specificity, Autoantibodies, Autoantigens, Autoimmune Diseases, Blotting, Dumortier, Enzyme-Linked Immunosorbent Assay, Genes, HLA-DP Antigens, HLA-DP beta-Chains, HLA-DQ Antigens, HLA-DQ beta-Chains, HLA-DR Antigens, HLA-DRB1 Chains, Humans, I2CT, MHC Class II, Peptides, Rheumatic Diseases, Ribonucleoprotein, Ribonucleoproteins, RNA-Binding Proteins, Small Nuclear, snRNP Core Proteins, Team-Dumortier, U1 Small Nuclear, Western
@article{dumortier_mhc_1999,
title = {MHC class II gene associations with autoantibodies to U1A and SmD1 proteins},
author = {H Dumortier and M Abbal and M Fort and J P Briand and A Cantagrel and S Muller},
doi = {10.1093/intimm/11.2.249},
issn = {0953-8178},
year = {1999},
date = {1999-01-01},
journal = {International Immunology},
volume = {11},
number = {2},
pages = {249--257},
abstract = {Autoantibodies against U small nuclear ribonucleoproteins (snRNP) are frequently present in the serum of patients with systemic rheumatic diseases, and have been reported to be associated with HLA-DR and -DQ genes. To better define the role of HLA genes in the production of such antibodies, we studied immunogenetic associations with autoantibodies reacting with U1 RNP, U1A and SmD1 proteins, and synthetic peptides containing immunodominant linear epitopes of these proteins. Only two out of the 15 overlapping peptides of U1A (i.e. peptides 35-58 and 257-282) and three of 11 peptides of SmD1 (i.e. peptides 1-20, 44-67 and 97-119) were significantly recognized by patients' sera selected on the basis of their antibody positivity with RNP in immunodiffusion. The distribution of DRB1, DQB1 and DPB1 alleles among the anti-RNP antibody-positive patients (n = 28) and healthy control subjects was similar. Antibodies against U1A (tested in Western immunoblotting with HeLa cell extracts) were positively associated to DRB1*06 allele; antibodies reacting with SmD1 peptide 44-67 were negatively associated to DRB1*02 and DQB1*0602 alleles. No association was found between DPB1 alleles and antibodies reacting with U1A and SmD1 antigens. This first study reporting an association between autoantibodies reacting with U1A and SmD1 proteins (and peptides of these proteins), and immunogenetic markers suggest that the production of antibody subsets directed against different components (or regions of these proteins) bound to the same snRNP particle is associated with distinct MHC class II alleles.},
keywords = {Alleles, Antibody Specificity, Autoantibodies, Autoantigens, Autoimmune Diseases, Blotting, Dumortier, Enzyme-Linked Immunosorbent Assay, Genes, HLA-DP Antigens, HLA-DP beta-Chains, HLA-DQ Antigens, HLA-DQ beta-Chains, HLA-DR Antigens, HLA-DRB1 Chains, Humans, I2CT, MHC Class II, Peptides, Rheumatic Diseases, Ribonucleoprotein, Ribonucleoproteins, RNA-Binding Proteins, Small Nuclear, snRNP Core Proteins, Team-Dumortier, U1 Small Nuclear, Western},
pubstate = {published},
tppubtype = {article}
}
1995
Briand J P, Guichard G, Dumortier H, Muller S
Retro-inverso peptidomimetics as new immunological probes. Validation and application to the detection of antibodies in rheumatic diseases Article de journal
Dans: The Journal of Biological Chemistry, vol. 270, no. 35, p. 20686–20691, 1995, ISSN: 0021-9258.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence, Animals, Antibodies, Autoantibodies, Autoimmune Diseases, Dumortier, Enzyme-Linked Immunosorbent Assay, Humans, I2CT, Immunoassay, Lupus Erythematosus, Mice, Molecular Sequence Data, Monoclonal, Peptide Fragments, Peptides, Rheumatic Diseases, Stereoisomerism, Structure-Activity Relationship, Systemic, Team-Dumortier
@article{briand_retro-inverso_1995,
title = {Retro-inverso peptidomimetics as new immunological probes. Validation and application to the detection of antibodies in rheumatic diseases},
author = {J P Briand and G Guichard and H Dumortier and S Muller},
doi = {10.1074/jbc.270.35.20686},
issn = {0021-9258},
year = {1995},
date = {1995-09-01},
journal = {The Journal of Biological Chemistry},
volume = {270},
number = {35},
pages = {20686--20691},
abstract = {Retro-inverso peptides which contain NH-CO bonds instead of CO-NH peptide bonds are much more resistant to proteolysis than L-peptides. Moreover, they have been shown recently to be able to mimic natural L-peptides with respect to poly- and monoclonal antibodies (Guichard, G., Benkirane, N., Zeder-Lutz, G., Van Regenmortel, M. H. V., Briand, J. P., and Muller, S. (1994b) Proc. Natl. Acad. Sci. U.S.A. 91, 9765-9769). We have further tested the capacity of retro-inverso peptidomimetics to serve as possible targets for antibodies produced by lupus mice and by patients with rheumatic autoimmune diseases. Several retro-inverso peptides corresponding to sequences known to be recognized by autoantibodies were synthesized, namely peptides 28-45 and 130-135 of H3, 277-291 of the Ro/SSA 52-kDa protein, and 304-324 of the Ro/SSA 60-kDa protein, and tested with autoimmune sera by enzyme-linked immunosorbent assay. We have found that retro-inverso peptides are recognized as well as or even better than natural peptides by antibodies from autoimmune patients and lupus mice. This new approach may lead to important progress in the future development of immunodiagnostic assays, particularly in the case of diseases characterized by inflammatory reactions in the course of which the level of degradative enzymes is increased.},
keywords = {Amino Acid Sequence, Animals, Antibodies, Autoantibodies, Autoimmune Diseases, Dumortier, Enzyme-Linked Immunosorbent Assay, Humans, I2CT, Immunoassay, Lupus Erythematosus, Mice, Molecular Sequence Data, Monoclonal, Peptide Fragments, Peptides, Rheumatic Diseases, Stereoisomerism, Structure-Activity Relationship, Systemic, Team-Dumortier},
pubstate = {published},
tppubtype = {article}
}