I2CT

@article{liu_drosophila_2012,

title = {Drosophila EYA regulates the immune response against DNA through an evolutionarily conserved threonine phosphatase motif},

author = {Xi Liu and Teruyuki Sano and Yongsheng Guan and Shigekazu Nagata and Jules A Hoffmann and Hidehiro Fukuyama},

doi = {10.1371/journal.pone.0042725},

issn = {1932-6203},

year  = {2012},

date = {2012-01-01},

journal = {PLoS ONE},

volume = {7},

number = {8},

pages = {e42725},

abstract = {Innate immune responses against DNA are essential to counter both pathogen infections and tissue damages. Mammalian EYAs were recently shown to play a role in regulating the innate immune responses against DNA. Here, we demonstrate that the unique Drosophila eya gene is also involved in the response specific to DNA. Haploinsufficiency of eya in mutants deficient for lysosomal DNase activity (DNaseII) reduces antimicrobial peptide gene expression, a hallmark for immune responses in flies. Like the mammalian orthologues, Drosophila EYA features a N-terminal threonine and C-terminal tyrosine phosphatase domain. Through the generation of a series of mutant EYA fly strains, we show that the threonine phosphatase domain, but not the tyrosine phosphatase domain, is responsible for the innate immune response against DNA. A similar role for the threonine phosphatase domain in mammalian EYA4 had been surmised on the basis of in vitro studies. Furthermore EYA associates with IKKβ and full-length RELISH, and the induction of the IMD pathway-dependent antimicrobial peptide gene is independent of SO. Our data provide the first in vivo demonstration for the immune function of EYA and point to their conserved immune function in response to endogenous DNA, throughout evolution.},

keywords = {Amino Acid, Animals, Blotting, Conserved Sequence, Endodeoxyribonucleases, Eye Proteins, hoffmann, Immunoprecipitation, M3i, Phosphoprotein Phosphatases, Sequence Homology, Transcription Factors, Western},

pubstate = {published},

tppubtype = {article}

}

@article{baeza_garcia_involvement_2010,

title = {Involvement of the cytokine MIF in the snail host immune response to the parasite Schistosoma mansoni},

author = {Alvaro Baeza Garcia and Raymond J Pierce and Benjamin Gourbal and Elisabeth Werkmeister and Dominique Colinet and Jean-Marc Reichhart and Colette Dissous and Christine Coustau},

doi = {10.1371/journal.ppat.1001115},

issn = {1553-7374},

year  = {2010},

date = {2010-01-01},

journal = {PLoS Pathog.},

volume = {6},

number = {9},

pages = {e1001115},

abstract = {We have identified and characterized a Macrophage Migration Inhibitory Factor (MIF) family member in the Lophotrochozoan invertebrate, Biomphalaria glabrata, the snail intermediate host of the human blood fluke Schistosoma mansoni. In mammals, MIF is a widely expressed pleiotropic cytokine with potent pro-inflammatory properties that controls cell functions such as gene expression, proliferation or apoptosis. Here we show that the MIF protein from B. glabrata (BgMIF) is expressed in circulating immune defense cells (hemocytes) of the snail as well as in the B. glabrata embryonic (Bge) cell line that has hemocyte-like features. Recombinant BgMIF (rBgMIF) induced cell proliferation and inhibited NO-dependent p53-mediated apoptosis in Bge cells. Moreover, knock-down of BgMIF expression in Bge cells interfered with the in vitro encapsulation of S. mansoni sporocysts. Furthermore, the in vivo knock-down of BgMIF prevented the changes in circulating hemocyte populations that occur in response to an infection by S. mansoni miracidia and led to a significant increase in the parasite burden of the snails. These results provide the first functional evidence that a MIF ortholog is involved in an invertebrate immune response towards a parasitic infection and highlight the importance of cytokines in invertebrate-parasite interactions.},

keywords = {Amino Acid, Animals, Apoptosis, Biomphalaria, Blotting, Cell Proliferation, Cells, Cricetinae, Cultured, Hemocytes, Host-Parasite Interactions, Humans, Liver, M3i, Macrophage Migration-Inhibitory Factors, messenger, Oocysts, Recombinant Proteins, reichhart, Reverse Transcriptase Polymerase Chain Reaction, RNA, Schistosoma mansoni, Schistosomiasis mansoni, Sequence Homology, Small Interfering, Western},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {IgG reactivity with a 100-kDa tissue and endothelial cell antigen identified as topoisomerase 1 distinguishes between limited and diffuse systemic sclerosis patients},

author = { P. Garcia de la Pena-Lefebvre and Y. Chanseaud and M. C. Tamby and J. Reinbolt and F. Batteux and Y. Allanore and A. Kahan and O. Meyer and O. Benveniste and O. Boyer and L. Guillevin and M. C. Boissier and L. Mouthon},

year  = {2004},

date = {2004-01-01},

journal = {Clin Immunol},

volume = {111},

number = {3},

pages = {241-51},

abstract = {We have analyzed antibody (Ab) reactivities of patients with limited systemic sclerosis (SSc) and anti-centromere Ab, patients with diffuse SSc and anti-topoisomerase 1 (anti-topo 1) Ab, patients with diffuse SSc without anti-topo 1 or anti-centromere Ab and age- and gender-matched healthy controls with normal human tissue and endothelial cell (EC) antigens. IgG reactivities with tissue antigens differed significantly between patients with anti-topo 1 Ab and patients with anti-centromere Ab. One 100-kDa band identified as topoisomerase 1 in macrovascular and microvascular EC extracts was recognized by IgG from patients with anti-topo 1 Ab and 50% of patients without specific Ab. IgG from patients with limited SSc and anti-centromere Ab, but not those of other patients or controls specifically recognized a 80-kDa band only in microvascular EC. Our results indicate that Ab from patients with limited or diffuse SSc with or without anti-topo 1 Ab exhibit specific and mutually exclusive reactivity patterns.},

note = {1521-6616 

Journal Article},

keywords = {Aged, Assay, Autoantibodies/*analysis, Blotting, Cells/*immunology, Centromere/immunology, DNA, EHRESMANN, Electrophoresis, Endothelial, Enzyme-Linked, Female, G/analysis, Gel, Gov't, Human, I/*immunology, Immunoglobulin, Immunosorbent, M/analysis, Male, Middle, Non-U.S., Polyacrylamide, Scleroderma, Support, Systemic/*immunology, Topoisomerases, Type, Western},

pubstate = {published},

tppubtype = {article}

}

@article{munier_pvf2_2002,

title = {PVF2, a PDGF/VEGF-like growth factor, induces hemocyte proliferation in Drosophila larvae},

author = {Anne-Isabelle Munier and Daniel Doucet and Emmanuel Perrodou and Daniel Zachary and Marie Meister and Jules A Hoffmann and Charles A Janeway and Marie Lagueux},

doi = {10.1093/embo-reports/kvf242},

issn = {1469-221X},

year  = {2002},

date = {2002-12-01},

journal = {EMBO Rep.},

volume = {3},

number = {12},

pages = {1195--1200},

abstract = {Blood cells play a crucial role in both morphogenetic and immunological processes in Drosophila, yet the factors regulating their proliferation remain largely unknown. In order to address this question, we raised antibodies against a tumorous blood cell line and identified an antigenic determinant that marks the surface of prohemocytes and also circulating plasmatocytes in larvae. This antigen was identified as a Drosophila homolog of the mammalian receptor for platelet-derived growth factor (PDGF)/vascular endothelial growth factor (VEGF). The Drosophila receptor controls cell proliferation in vitro. By overexpressing in vivo one of its putative ligands, PVF2, we induced a dramatic increase in circulating hemocytes. These results identify the PDGF/VEGF receptor homolog and one of its ligands as important players in Drosophila hematopoiesis.},

keywords = {Animals, Antibodies, Blotting, Cell Differentiation, Hemocytes, hoffmann, Immunohistochemistry, Larva, ligands, M3i, Platelet-Derived Growth Factor, Receptors, Vascular Endothelial Growth Factor, Western},

pubstate = {published},

tppubtype = {article}

}

@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}

}