Publications
2005
Monneaux Fanny, Hoebeke Johan, Sordet Christelle, Nonn Céline, Briand Jean-Paul, Maillère Bernard, Sibilia Jean, Muller Sylviane
Selective modulation of CD4+ Ŧ cells from lupus patients by a promiscuous, protective peptide analog Article de journal
Dans: Journal of Immunology (Baltimore, Md.: 1950), vol. 175, no. 9, p. 5839–5847, 2005, ISSN: 0022-1767.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence, CD4-Positive T-Lymphocytes, HLA-DR Antigens, Humans, I2CT, Interleukin-10, Lupus Erythematosus, Lymphocyte Activation, Molecular Sequence Data, Monneaux, Peptide Fragments, Phosphorylation, Ribonucleoprotein, Systemic, Team-Dumortier, U1 Small Nuclear
@article{monneaux_selective_2005,
title = {Selective modulation of CD4+ Ŧ cells from lupus patients by a promiscuous, protective peptide analog},
author = {Fanny Monneaux and Johan Hoebeke and Christelle Sordet and Céline Nonn and Jean-Paul Briand and Bernard Maillère and Jean Sibilia and Sylviane Muller},
doi = {10.4049/jimmunol.175.9.5839},
issn = {0022-1767},
year = {2005},
date = {2005-11-01},
journal = {Journal of Immunology (Baltimore, Md.: 1950)},
volume = {175},
number = {9},
pages = {5839--5847},
abstract = {A peptide encompassing residues 131-151 of the spliceosomal U1-70K protein and its analog phosphorylated at Ser140 were synthesized as potential candidates for the treatment of patients with lupus. Studies in the MRL/lpr and (NZB x NZW)F1 lupus models have demonstrated that these sequences contain a CD4+ T cell epitope but administration of the phosphorylated peptide only ameliorates the clinical manifestations of treated MRL/lpr mice. Binding assays with soluble HLA class II molecules and molecular modeling experiments indicate that both peptides behave as promiscuous epitopes and bind to a large panel of human DR molecules. In contrast to normal T cells and T cells from non-lupus autoimmune patients, we found that PBMCs from 40% of lupus patients selected randomly and CFSE-labeled CD4+ T cells proliferate in response to peptide 131-151. Remarkably, however, we observed that phosphorylation of Ser140 prevents CD4+ T cells proliferation but not secretion of regulatory cytokines, suggesting a striking immunomodulatory effect of phosphorylated analog on lupus CD4+ T cells that was unique to patients. The analog might act as an activator of regulatory T cells or as a partial agonist of TCR.},
keywords = {Amino Acid Sequence, CD4-Positive T-Lymphocytes, HLA-DR Antigens, Humans, I2CT, Interleukin-10, Lupus Erythematosus, Lymphocyte Activation, Molecular Sequence Data, Monneaux, Peptide Fragments, Phosphorylation, Ribonucleoprotein, Systemic, Team-Dumortier, U1 Small Nuclear},
pubstate = {published},
tppubtype = {article}
}
Berthier-Vergnes Odile, Bermond Fabienne, Flacher Vincent, Massacrier Catherine, Schmitt Daniel, Péguet-Navarro Josette
TNF-alpha enhances phenotypic and functional maturation of human epidermal Langerhans cells and induces IL-12 p40 and IP-10/CXCL-10 production Article de journal
Dans: FEBS letters, vol. 579, no. 17, p. 3660–3668, 2005, ISSN: 0014-5793.
Résumé | Liens | BibTeX | Étiquettes: Antigens, Apoptosis, C-Type, CD, Cell Differentiation, Cells, Chemokine CXCL10, chemokines, Cultured, CXC, Epidermal Cells, HLA-DR Antigens, Humans, Hypersensitivity, Interleukin-12, Interleukin-12 Subunit p40, Langerhans Cells, Lectins, Mannose-Binding Lectins, Phenotype, Protein Subunits, Surface, T-Lymphocytes, Team-Mueller, Tumor Necrosis Factor-alpha
@article{berthier-vergnes_tnf-alpha_2005,
title = {TNF-alpha enhances phenotypic and functional maturation of human epidermal Langerhans cells and induces IL-12 p40 and IP-10/CXCL-10 production},
author = {Odile Berthier-Vergnes and Fabienne Bermond and Vincent Flacher and Catherine Massacrier and Daniel Schmitt and Josette Péguet-Navarro},
doi = {10.1016/j.febslet.2005.04.087},
issn = {0014-5793},
year = {2005},
date = {2005-07-01},
journal = {FEBS letters},
volume = {579},
number = {17},
pages = {3660--3668},
abstract = {Dendritic cells (DC) play a central role in immunity/tolerance decision, depending on their activation/maturation state. TNF-alpha is largely produced in the skin under inflammatory conditions. However, it still remains to be defined how TNF-alpha modulates the activation status of human LC, the most specialized DC controlling skin immunity. Here, we reported that fresh immature LC, highly purified from healthy human skin and exposed for two days to TNF-alpha under serum-free conditions, expressed up-regulated level of co-stimulatory molecules (CD40, CD54, CD86), maturation markers (CD83, DC-LAMP), CCR7 lymph node homing receptor, and down-regulated Langerin level, in a dose-dependent manner. This mature phenotype is closely associated with enhanced LC allostimulatory capacity. Furthermore, TNF-alpha significantly increased the number of viable LC and decreased their spontaneous apoptosis. More importantly, TNF-alpha induced LC to produce both IFN-gamma-inducible-protein IP-10/CXCL10, a Th1-attracting chemokine and IL-12 p40. Bioactive IL-12 p70 was never detected, even after additional CD40 stimulus. The results implicate LC as an effective target through which TNF-alpha may up- or down-regulate the inflammatory skin reactions.},
keywords = {Antigens, Apoptosis, C-Type, CD, Cell Differentiation, Cells, Chemokine CXCL10, chemokines, Cultured, CXC, Epidermal Cells, HLA-DR Antigens, Humans, Hypersensitivity, Interleukin-12, Interleukin-12 Subunit p40, Langerhans Cells, Lectins, Mannose-Binding Lectins, Phenotype, Protein Subunits, Surface, T-Lymphocytes, Team-Mueller, Tumor Necrosis Factor-alpha},
pubstate = {published},
tppubtype = {article}
}
2003
Monneaux Fanny, Lozano José Manuel, Patarroyo Manuel E, Briand Jean-Paul, Muller Sylviane
T cell recognition and therapeutic effect of a phosphorylated synthetic peptide of the 70K snRNP protein administered in MR/lpr mice Article de journal
Dans: European Journal of Immunology, vol. 33, no. 2, p. 287–296, 2003, ISSN: 0014-2980.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence, Animal, Animals, Autoantibodies, Autoantigens, Autoimmune Diseases, B-Lymphocytes, Cross Reactions, Disease Models, Female, HLA-DR Antigens, HLA-DR Serological Subtypes, HLA-DR1 Antigen, HLA-DR4 Antigen, Humans, I2CT, Immunization, Immunotherapy, Inbred BALB C, Inbred MRL lpr, Lupus Erythematosus, Lupus Nephritis, Mice, Molecular Sequence Data, Monneaux, Peptide Fragments, Phosphorylation, Protein Binding, Ribonucleoprotein, Systemic, T-Lymphocytes, Team-Dumortier, U1 Small Nuclear
@article{monneaux_t_2003,
title = {T cell recognition and therapeutic effect of a phosphorylated synthetic peptide of the 70K snRNP protein administered in MR/lpr mice},
author = {Fanny Monneaux and José Manuel Lozano and Manuel E Patarroyo and Jean-Paul Briand and Sylviane Muller},
doi = {10.1002/immu.200310002},
issn = {0014-2980},
year = {2003},
date = {2003-01-01},
journal = {European Journal of Immunology},
volume = {33},
number = {2},
pages = {287--296},
abstract = {Modifications of self antigens that occur during apoptosis might be involved in the generation of neo-antigens, which can break tolerance and induce autoimmunity. We have previously identified an epitope at residues 131-151 of the U1-70K snRNP protein, recognized by IgG antibodies and CD4+ T cells from at least two strains of lupus mice. With the aim of investigating the possible role of phosphorylation on the antigenicity of peptide 131-151 and to gain a better understanding of how this peptide can drive autoimmune response, we synthesized two peptides phosphorylated on Ser137 and 140, respectively. We show here that peptide P140 phosphorylated on Ser140 is recognized by both CD4+ T cells and antibodies from MRL/lpr mice. Furthermore, intravenous administration to lupus-prone MRL/lpr mice of P140 in saline (but not of the non-phosphorylated peptide) decreased proteinuria and anti-DNA antibody production, and significantly prolonged survival of treated mice. We further demonstrated that P140 is recognized by antibodies from lupus patients and binds to various HLA DR molecules, offering new hope for manipulating T cell response in humans.},
keywords = {Amino Acid Sequence, Animal, Animals, Autoantibodies, Autoantigens, Autoimmune Diseases, B-Lymphocytes, Cross Reactions, Disease Models, Female, HLA-DR Antigens, HLA-DR Serological Subtypes, HLA-DR1 Antigen, HLA-DR4 Antigen, Humans, I2CT, Immunization, Immunotherapy, Inbred BALB C, Inbred MRL lpr, Lupus Erythematosus, Lupus Nephritis, Mice, Molecular Sequence Data, Monneaux, Peptide Fragments, Phosphorylation, Protein Binding, Ribonucleoprotein, Systemic, T-Lymphocytes, Team-Dumortier, U1 Small Nuclear},
pubstate = {published},
tppubtype = {article}
}
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}
}