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Start Over Author "Immunité et cancer ( U932 )" Publisher proceedings of the national academy of sciences
3 results on '"Immunité et cancer ( U932 )"'

1. Restricting nonclassical MHC genes coevolve with TRAV genes used by innate-like T cells in mammals

Author

Luc Jouneau, Marie-Paule Lefranc, Luc Teyton, Stanislas Mondot, Olivier Lantz, Pierre Boudinot, ProdInra, Migration, Unité de recherche Virologie et Immunologie Moléculaires (VIM (UR 0892)), Institut National de la Recherche Agronomique (INRA), Université Paris Saclay (COmUE), Immunité et cancer (U932), Université Paris Descartes - Paris 5 (UPD5)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Immunology and Microbial Science, The Scripps Research Institute [La Jolla, San Diego], Institut de génétique humaine (IGH), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut Gustave Roussy (IGR), Laboratoire d'Immunologie Clinique, Institut Curie [Paris], Centre d'Investigation Clinique en Biotherapie des cancers (CIC 1428 , CBT 507 ), Institut Gustave Roussy (IGR)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Scripps Research Institute, and Institut Gustave Roussy (IGR)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
0301 basic medicine, Receptors, Antigen, T-Cell, alpha-beta, T-Lymphocytes, [SDV]Life Sciences [q-bio], Complementarity determining region, Major histocompatibility complex, Evolution, Molecular, 03 medical and health sciences, Negative selection, 0302 clinical medicine, evolution, Animals, mammals, Gene, Genetics, Multidisciplinary, biology, Histocompatibility Antigens Class I, T-cell receptor, RNA, Natural killer T cell, Complementarity Determining Regions, [SDV] Life Sciences [q-bio], 030104 developmental biology, PNAS Plus, CD1D, Cats, biology.protein, Rabbits, MHC, MAIT, TCR, 030215 immunology
Abstract

International audience; Whereas major histocompatibility class-1 (MH1) proteins present peptides to T cells displaying a large T-cell receptor (TR) repertoire, MH1Like proteins, such as CD1D and MR1, present glycolipids and microbial riboflavin precursor derivatives, respectively, to T cells expressing invariant TR-α (iTRA) chains. The groove of such MH1Like, as well as iTRA chains used by mucosal-associated invariant T (MAIT) and natural killer T (NKT) cells, respectively, may result from a coevolution under particular selection pressures. Herein, we investigated the evolutionary patterns of the iTRA of MAIT and NKT cells and restricting MH1Like proteins: MR1 appeared 170 Mya and is highly conserved across mammals, evolving more slowly than other MH1Like. It has been pseudogenized or independently lost three times in carnivores, the armadillo, and lagomorphs. The corresponding TRAV1 gene also evolved slowly and harbors highly conserved complementarity determining regions 1 and 2. TRAV1 is absent exclusively from species in which MR1 is lacking, suggesting that its loss released the purifying selection on MR1. In the rabbit, which has very few NKT and no MAIT cells, a previously unrecognized iTRA was identified by sequencing leukocyte RNA. This iTRA uses TRAV41, which is highly conserved across several groups of mammals. A rabbit MH1Like gene was found that appeared with mammals and is highly conserved. It was independently lost in a few groups in which MR1 is present, like primates and Muridae, illustrating compensatory emergences of new MH1Like/Invariant T-cell combinations during evolution. Deciphering their role is warranted to search similar effector functions in humans.

Published
2016

2. Autonomous phagosomal degradation and antigen presentation in dendritic cells

Author

Fiorella Kotsias, Eik Hoffmann, Sebastian Amigorena, Ariel Savina, Pierre Bruhns, Geraldine Visentin, Immunité et cancer (U932), Université Paris Descartes - Paris 5 (UPD5)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Anticorps en Thérapie et Pathologie, Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Immunité et cancer, Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was financed by Institut Curie, Institut National de la Santé et de la Recherche Médicale, Association pour la Recherche sur le Cancer (Grant SFI20101201629), La Ligue Nationale contre le Cancer (Ligue Labellisée 2007–2010 and 2011–2013), the European Research Council (Grant PhagoDC 233062), Agence National de Recherche (MIME, APAT), and the Bettencourt-Schueller Foundation. E.H. was supported by grants from Fondation Recherche Médicale and the AXA Research Fund, F.K. was supported by the European Research Council, and A.S. was supported by the Association pour la Recherche sur le Cancer., ANR-07-MIME-0002,APAT,Presentation croisée et activation des lymphocytes T par les cellules dendritiques(2007), European Project: 233062,EC:FP7:ERC,ERC-2008-AdG,PHAGODC(2009), Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Curie [Paris], Martin, Marie, Microbiologie, immunologie et maladies émergentes - Presentation croisée et activation des lymphocytes T par les cellules dendritiques - - APAT2007 - ANR-07-MIME-0002 - MIME - VALID, Integrative phagosomal biology: antigen presentation and developmental programs in dendritic cells - PHAGODC - - EC:FP7:ERC2009-07-01 - 2014-06-30 - 233062 - VALID, and Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
[SDV.IMM] Life Sciences [q-bio]/Immunology, Ovalbumin, Antigen presentation, MESH: Microspheres, MESH: Flow Cytometry, Immunoglobulin G, Mice, 03 medical and health sciences, MESH: Phagosomes, 0302 clinical medicine, Immune system, Phagocytosis, Antigen, Phagosomes, Animals, MESH: Animals, MESH: Phagocytosis, MESH: Mice, MESH: Opsonin Proteins, 030304 developmental biology, Phagosome, MESH: Immunoglobulin G, Antigen Presentation, 0303 health sciences, MESH: Ovalbumin, Multidisciplinary, MESH: Dendritic Cells, biology, Antigen processing, Dendritic Cells, Biological Sciences, Opsonin Proteins, Flow Cytometry, Acquired immune system, Microspheres, Cell biology, Antibody opsonization, 030220 oncology & carcinogenesis, MESH: Antigen Presentation, biology.protein, [SDV.IMM]Life Sciences [q-bio]/Immunology, Lysosomes, MESH: Lysosomes
Abstract

This article contains supporting information online at : www.pnas.org/lookup/suppl/doi:10.1073/pnas.1203912109/-/DCSupplemental; International audience; Phagocytosis plays a critical role in both innate and adaptive immunity. Phagosomal fusion with late endosomes and lysosomes enhances proteolysis, causing degradation of the phagocytic content. Increased degradation participates in both innate protection against pathogens and the production of antigenic peptides for presentation to T lymphocytes during adaptive immune responses. Specific ligands present in the phagosomal cargo influence the rate of phagosome fusion with lysosomes, thereby modulating both antigen degradation and presentation. Using a combination of cell sorting techniques and single phagosome flow cytometry-based analysis, we found that opsonization with IgG accelerates antigen degradation within individual IgG-containing phagosomes, but not in other phagosomes present in the same cell and devoid of IgG. Likewise, IgG opsonization enhances antigen presentation to CD4(+) T lymphocytes only when antigen and IgG are present within the same phagosome, whereas cells containing phagosomes with either antigen or IgG alone failed to present antigen efficiently. Therefore, individual phagosomes behave autonomously, in terms of both cargo degradation and antigen presentation to CD4(+) T cells. Phagosomal autonomy could serve as a basis for the intracellular discrimination between self and nonself antigens, resulting in the preferential presentation of peptides derived from opsonized, nonself antigens.

Published
2012

3. Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A

Author

Christophe Cans, Nathalie Amzallag, Manuela Argentini, Adam Telerman, David Allanic, Dino Moras, V. F. Shalak, Marc Mirande, Bruno Goud, Virginie Crible, Giusy Fiucci, Vanessa Nancy-Portebois, Brent Passer, Robert Amson, Rowena Tufino, State Key Laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, Immunité et cancer (U932), Université Paris Descartes - Paris 5 (UPD5)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Chimie des Substances Naturelles (ICSN), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Organisation Reconstruction Travail - ORT (FRANCE), Compartimentation et dynamique cellulaires (CDC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'Enzymologie et Biochimie Structurales (LEBS), Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie et de Pharmacologie Appliquée (LBPA), École normale supérieure - Cachan (ENS Cachan)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), Université Paris Descartes - Paris 5 (UPD5)-Institut Curie-Institut National de la Santé et de la Recherche Médicale (INSERM), and Centre National de la Recherche Scientifique (CNRS)-Institut Curie-Université Pierre et Marie Curie - Paris 6 (UPMC)

Subjects
Guanine, Recombinant Fusion Proteins, [SDV]Life Sciences [q-bio], [SDV.CAN]Life Sciences [q-bio]/Cancer, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, GTPase, In Vitro Techniques, Guanosine Diphosphate, 03 medical and health sciences, chemistry.chemical_compound, Peptide Elongation Factor 1, 0302 clinical medicine, Drug Stability, Two-Hybrid System Techniques, Translationally-controlled tumor protein, Biomarkers, Tumor, Protein biosynthesis, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Guanine Nucleotide Dissociation Inhibitors, 030304 developmental biology, 0303 health sciences, Multidisciplinary, biology, Tumor Protein, Translationally-Controlled 1, Biological Sciences, Guanine Nucleotides, Kinetics, Biochemistry, chemistry, Guanosine diphosphate, Protein Biosynthesis, 030220 oncology & carcinogenesis, biology.protein, Translationally controlled tumour protein, Guanine nucleotide exchange factor
Abstract

Recently, we demonstrated that the expression levels of the translationally controlled tumor protein (TCTP) were strongly down-regulated at the mRNA and protein levels during tumor reversion/suppression and by the activation of p53 and Siah-1. To better characterize the function of TCTP, a yeast two-hybrid hunt was performed. Subsequent analysis identified the translation elongation factor, eEF1A, and its guanine nucleotide exchange factor, eEF1Bβ, as TCTP-interacting partners. In vitro and in vivo studies confirmed that TCTP bound specifically eEF1Bβ and eEF1A. Additionally, MS analysis also identified eEF1A as a TCTP interactor. Because eEF1A is a GTPase, we investigated the role of TCTP on the nucleotide exchange reaction of eEF1A. Our results show that TCTP preferentially stabilized the GDP form of eEF1A, and, furthermore, impaired the GDP exchange reaction promoted by eEF1Bβ. These data suggest that TCTP has guanine nucleotide dissociation inhibitor activity, and, moreover, implicate TCTP in the elongation step of protein synthesis.

Published
2003

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