105 results on '"Battini, Jean-Luc"'
Search Results
2. A co-opted endogenous retroviral envelope promotes cell survival by controlling CTR1-mediated copper transport and homeostasis
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Tury, Sandrine, Chauveau, Lise, Lecante, Arnaud, Courgnaud, Valérie, and Battini, Jean-Luc
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- 2023
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3. Glucose Transporter 1 Expression Identifies a Population of Cycling CD4 + CD8 + Human Thymocytes with High CXCR4-Induced Chemotaxis
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Swainson, Louise, Kinet, Sandrina, Manel, Nicolas, Battini, Jean-Luc, Sitbon, Marc, Taylor, Naomi, and Herzenberg, Leonard A.
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- 2005
4. Precise Gene Localization by Phenotypic Assay of Radiation Hybrid Cells
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Battini, Jean-Luc, Kruglyak, Leonid, Cox, David R., and Miller, A. Dusty
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- 2000
5. The RD114/Simian Type D Retrovirus Receptor Is a Neutral Amino Acid Transporter
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Battini, Jean-Luc, Gottschalk, Rebecca J., Mazo, Ilya, and Miller, A. Dusty
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- 1999
6. A Human Cell-Surface Receptor for Xenotropic and Polytropic Murine Leukemia Viruses: Possible Role in G Protein-Coupled Signal Transduction
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Battini, Jean-Luc and Miller, A. Dusty
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- 1999
7. Characterization of XPR1/SLC53A1 variants located outside of the SPX domain in patients with primary familial brain calcification
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López-Sánchez, Uriel, Nicolas, Gaël, Richard, Anne-Claire, Maltête, David, Charif, Mahmoud, Ayrignac, Xavier, Goizet, Cyril, Touhami, Jawida, Labesse, Gilles, Battini, Jean-Luc, and Sitbon, Marc
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- 2019
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8. XPR1 mutations are a rare cause of primary familial brain calcification
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Anheim, Mathieu, López-Sánchez, Uriel, Giovannini, Donatella, Richard, Anne-Claire, Touhami, Jawida, N’Guyen, Ludovic, Rudolf, Gabrielle, Thibault-Stoll, Anne, Frebourg, Thierry, Hannequin, Didier, Campion, Dominique, Battini, Jean-Luc, Sitbon, Marc, and Nicolas, Gaël
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- 2016
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9. Optimization of tumor xenograft dissociation for the profiling of cell surface markers and nutrient transporters
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Petit, Vincent, Massonnet, Gérald, Maciorowski, Zofia, Touhami, Jawida, Thuleau, Aurélie, Némati, Fariba, Laval, Julie, Château-Joubert, Sophie, Servely, Jean-Luc, Vallerand, David, Fontaine, Jean-Jacques, Taylor, Naomi, Battini, Jean-Luc, Sitbon, Marc, and Decaudin, Didier
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- 2013
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10. Glut1-mediated glucose transport regulates HIV infection
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Loisel-Meyer, Séverine, Swainson, Louise, Craveiro, Marco, Oburoglu, Leal, Mongellaz, Cédric, Costa, Caroline, Martinez, Marion, Cosset, François-Loic, Battini, Jean-Luc, Herzenberg, Leonard A., Herzenberg, Leonore A., Atkuri, Kondala R., Sitbon, Marc, Kinet, Sandrina, Verhoeyen, Els, and Taylor, Naomi
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- 2012
11. Preface
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Souza Ribeiro de Oliveira, Lucia Marisy, Burte, Julien, Martins, Eduardo Savio, and Battini, Jean-Luc
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- 2022
12. Mouse retroviruses and chronic fatigue syndrome: Does X (or P) mark the spot?
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Courgnaud, Valerie, Battini, Jean-Luc, Sitbon, Marc, and Mason, Andrew L.
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- 2010
13. Mechanism for XMRV neurotoxicity
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Miller A Dusty, Battini Jean-Luc, Aranda Ramona, Mendoza Ramon, and Vaughan Andrew E
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Immunologic diseases. Allergy ,RC581-607 - Published
- 2011
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14. HTLV-1 tropism and envelope receptor
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Manel, Nicolas, Battini, Jean-Luc, Taylor, Naomi, and Sitbon, Marc
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- 2005
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15. Glucose transporter 1 expression identifies a population of cyclin CD[4.sup.+]CD[8.sup.+] human thymocytes with high CXCR4-induced chemotaxis
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Swainson, Louise, Kinet, Sandrina, Manel, Nicolas, Battini, Jean-Luc, Sitbon, Marc, and Taylor, Naomi
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Metabolism -- Research ,T cells -- Research ,Lymphocytes -- Research ,Dextrose -- Research ,Glucose -- Research ,Science and technology - Abstract
GLUT1, the major glucose transporter in peripheral T lymphocytes, is induced upon T cell receptor activation. However, the role of GLUT1 during human thymocyte differentiation remains to be evaluated. Our identification of GLUT1 as the human T lymphotrophic virus (HTLV) receptor has enabled us to use tagged HTLV-receptor-binding domain fusion proteins to specifically monitor surface GLUT1 expression. Here, we identify a unique subset of CD[4.sup.+]CD[8.sup.+] double-positive (DP) thymocytes, based on their GLUT1 surface expression. Whereas these cells express variable levels of CD8, they express uniformly high levels of CD4. Glucose uptake was 7-fold higher in CD[4.sup.hi]Dp thymocytes than in CD[4.sup.lo]DP thymocytes (P = 0.0002). Further analyses indicated that these GLUT[1.sup.+] thymocytes are early post-[beta]-selection, as demonstrated by low levels of T cell receptor (TCR)[alpha][beta] and CD3. This population of immature GLUT[1.sup.+]DP cells is rapidly cycling and can be further distinguished by specific expression of the transferrin receptor. Importantly, the CXCR4 chemokine receptor is expressed at 15-fold higher levels on GLUT1+DP thymocytes, as compared with the DP GLUT[1.sup.-] subset, and the former cells show enhanced chemotaxis to the CXCR4 ligand CXCL12. Thus, during human thymopoiesis, GLUT1 is up-regulated after [beta]-selection, and these immature DP cells constitute a population with distinct metabolic and chemotactic properties. GLUT-1 | metabolism | thymus
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- 2005
16. Capture in the metabolic arena: co-selection of gamma and deltaretrovirus envelope glycoproteins and their receptors
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Battini Jean-Luc, Roumestand Christian, de Guillen Karine, Nadal-Desbarats Lydie, Lagrue Emmanuelle, Switzer Wiliam M, Castelnau Pierre, Touhami Jawida, Manel Nicolas, Lavanya Madakasira, Kim Felix, Giovannini Donatella, Courgnaud Valérie, Abe Hiroyuki, and Sitbon Marc
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Immunologic diseases. Allergy ,RC581-607 - Published
- 2009
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17. The HTLV receptor is an early T-cell activation marker whose expression requires de novo protein synthesis
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Manel, Nicolas, Kinet, Sandrina, Battini, Jean-Luc, Kim, Felix J., Taylor, Naomi, and Sitbon, Marc
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- 2003
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18. Cyclophilins and nucleoporins are required for infection mediated by capsids from circulating HIV-2 primary isolates
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Mamede, João, Damond, Florence, Bernardo, Ariel de, Matheron, Sophie, Descamps, Diane, Battini, Jean-Luc, Sitbon, Marc, Courgnaud, Valérie, Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Hôpital Bichat - Claude Bernard, Laboratoire de Virologie, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-AP-HP - Hôpital Bichat - Claude Bernard [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Recherches Translationnelles sur le VIH et les maladies infectieuses endémiques er émergentes (TransVIHMI), Université Cheikh Anta Diop [Dakar, Sénégal] (UCAD)-Institut de Recherche pour le Développement (IRD)-Université de Yaoundé I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Université Montpellier 1 (UM1), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Recherches Translationnelles sur le VIH et les maladies infectieuses endémiques et émergentes (TransVIHMI), and Institut de Recherche pour le Développement (IRD)-Université de Yaoundé I-Université Cheikh Anta Diop [Dakar, Sénégal] (UCAD)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)
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Cell Nucleus ,Ubiquitin-Protein Ligases ,virus diseases ,HIV Infections ,[SDV.BC]Life Sciences [q-bio]/Cellular Biology ,Virus Replication ,Article ,Antiviral Restriction Factors ,Nuclear Pore Complex Proteins ,Tripartite Motif Proteins ,Africa, Western ,Mice ,Capsid ,HEK293 Cells ,HIV-2 ,[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology ,[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB] ,HIV-1 ,Animals ,Humans ,Carrier Proteins ,Cyclophilin A ,ComputingMilieux_MISCELLANEOUS ,Molecular Chaperones - Abstract
HIV-2 groups have emerged from sooty mangabey SIV and entered the human population in Africa on several separate occasions. Compared to world pandemic HIV-1 that arose from the chimpanzee SIVcpz virus, the SIVsm-derived HIV-2, largely confined to West Africa, is less replicative, less transmissible and less pathogenic. Here, we evaluated the interactions between host cellular factors, which control HIV-1 infection and target the capsid, and HIV-2 capsids obtained from primary isolates from patients with different disease progression status. We showed that, like HIV-1, all HIV-2 CA we tested exhibited a dependence on cyclophilin A. However, we observed no correlation between HIV-2 viremia and susceptibility to hu-TRIM5alpha or dependence to CypA. Finally, we found that all CA from HIV-2 primary isolates exploit Nup358 and Nup153 for nucleus transposition. Altogether, these findings indicate that the ability to use the two latter nucleoporins is essential to infection of human cells for both HIV-1 and HIV-2. This dependence provides another molecular target that could be used for antiviral strategies against both HIV-1 and 2, based on both nucleoporins.
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- 2017
19. Regional characterization of energy metabolism in the brain of normal and MPTP-intoxicated mice using new markers of glucose and phosphate transport
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Touhami Jawida, Lavanya Madakasira, Abe Hiroyuki, Lagrue Emmanuelle, Bodard Sylvie, Chalon Sylvie, Battini Jean-Luc, Sitbon Marc, and Castelnau Pierre
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Medicine - Abstract
Abstract The gibbon ape leukemia virus (GALV), the amphotropic murine leukemia virus (AMLV) and the human T-cell leukemia virus (HTLV) are retroviruses that specifically bind nutrient transporters with their envelope glycoproteins (Env) when entering host cells. Here, we used tagged ligands derived from GALV, AMLV, and HTLV Env to monitor the distribution of their cognate receptors, the inorganic phosphate transporters PiT1 and PiT2, and the glucose transporter GLUT1, respectively, in basal conditions and after acute energy deficiency. For this purpose, we monitored changes in the distribution of PiT1, PiT2 and GLUT1 in the cerebellum, the frontal cortex, the corpus callosum, the striatum and the substantia nigra (SN) of C57/BL6 mice after administration of 1-methyl-4-phenyl-1,2,3,6 tetrahydropyridinium (MPTP), a mitochondrial complex I inhibitor which induces neuronal degeneration in the striato-nigral network. The PiT1 ligand stained oligodendrocytes in the corpus callosum and showed a reticular pattern in the SN. The PiT2 ligand stained particularly the cerebellar Purkinje cells, while GLUT1 labelling was mainly observed throughout the cortex, basal ganglia and cerebellar gray matter. Interestingly, unlike GLUT1 and PiT2 distributions which did not appear to be modified by MPTP intoxication, PiT1 immunostaining seemed to be more extended in the SN. The plausible reasons for this change following acute energy stress are discussed. These new ligands therefore constitute new metabolic markers which should help to unravel cellular adaptations to a wide variety of normal and pathologic conditions and to determine the role of specific nutrient transporters in tissue homeostasis.
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- 2010
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20. Isolated receptor binding domains of HTLV-1 and HTLV-2 envelopes bind Glut-1 on activated CD4+ and CD8+ T cells
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Montel-Hagen Amélie, Mongellaz Cedric, Lavanya Madakasira, Swainson Louise, Kinet Sandrina, Craveiro Marco, Manel Nicolas, Battini Jean-Luc, Sitbon Marc, and Taylor Naomi
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Immunologic diseases. Allergy ,RC581-607 - Abstract
Abstract Background We previously identified the glucose transporter Glut-1, a member of the multimembrane-spanning facilitative nutrient transporter family, as a receptor for both HTLV-1 and HTLV-2. However, a recent report concluded that Glut-1 cannot serve as a receptor for HTLV-1 on CD4 T cells: This was based mainly on their inability to detect Glut-1 on this lymphocyte subset using the commercial antibody mAb1418. It was therefore of significant interest to thoroughly assess Glut-1 expression on CD4 and CD8 T cells, and its association with HTLV-1 and -2 envelope binding. Results As previously reported, ectopic expression of Glut-1 but not Glut-3 resulted in significantly augmented binding of tagged proteins harboring the receptor binding domains of either HTLV-1 or HTLV-2 envelope glycoproteins (H1RBD or H2RBD). Using antibodies raised against the carboxy-terminal peptide of Glut-1, we found that Glut-1 expression was significantly increased in both CD4 and CD8 cells following TCR stimulation. Corresponding increases in the binding of H1RBD as well as H2RBD, not detected on quiescent T cells, were observed following TCR engagement. Furthermore, increased Glut-1 expression was accompanied by a massive augmentation in glucose uptake in TCR-stimulated CD4 and CD8 lymphocytes. Finally, we determined that the apparent contradictory results obtained by Takenouchi et al were due to their monitoring of Glut-1 with a mAb that does not bind cells expressing endogenous Glut-1, including human erythrocytes that harbor 300,000 copies per cell. Conclusion Transfection of Glut-1 directly correlates with the capacities of HTLV-1 and HTLV-2 envelope-derived ligands to bind cells. Moreover, Glut-1 is induced by TCR engagement, resulting in massive increases in glucose uptake and binding of HTLV-1 and -2 envelopes to both CD4 and CD8 T lymphocytes. Therefore, Glut-1 is a primary binding receptor for HTLV-1 and HTLV-2 envelopes on activated CD4 as well as CD8 lymphocytes.
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- 2007
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21. Intrahost variations in the envelope receptor-binding domain (RBD) of HTLV-1 and STLV-1 primary isolates
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Sitbon Marc, Battini Jean-Luc, Gallego Sandra, Gessain Antoine, Lavanya Madakasira, Kim Felix J, and Courgnaud Valérie
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Immunologic diseases. Allergy ,RC581-607 - Abstract
Abstract Four primate (PTLV), human (HTLV) and simian (STLV) T-cell leukemia virus types, have been characterized thus far, with evidence of a simian zoonotic origin for HTLV-1, HTLV-2 and HTLV-3 in Africa. The PTLV envelope glycoprotein surface component (SUgp46) comprises a receptor-binding domain (RBD) that alternates hypervariable and highly conserved sequences. To further delineate highly conserved motifs in PTLV RBDs, we investigated the intrahost variability of HTLV-1 and STLV-1 by generating and sequencing libraries of DNA fragments amplified within the RBD of the SUgp46 env gene. Using new and highly cross-reactive env primer pairs, we observed the presence of Env quasispecies in HTLV-1 infected individuals and STLV-1 naturally infected macaques, irrespective of the clinical status. These intrahost variants helped us to define highly conserved residues and motifs in the RBD. The new highly sensitive env PCR described here appears suitable for the screening of all known variants of the different PTLV types and should, therefore, be useful for the analysis of seroindeterminate samples.
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- 2006
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22. HTLV-1 and -2 envelope SU subdomains and critical determinants in receptor binding
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Valle Carine, Garrido Edith N, Manel Nicolas, Kim Felix J, Sitbon Marc, and Battini Jean-Luc
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Immunologic diseases. Allergy ,RC581-607 - Abstract
Abstract Background Human T-cell leukemia virus (HTLV) -1 and -2 are deltaretroviruses that infect a wide range of cells. Glut1, the major vertebrate glucose transporter, has been shown to be the HTLV Env receptor. While it is well established that the extracellular surface component (SU) of the HTLV envelope glycoprotein (Env) harbors all of the determinants of interaction with the receptor, identification of SU subdomains that are necessary and sufficient for interaction with the receptor, as well as critical amino acids therein, remain to be precisely defined. Although highly divergent in the rest of their genomes, HTLV and murine leukemia virus (MLV) Env appear to be related and based on homologous motifs between the HTLV and MLV SU, we derived chimeric HTLV/MLV Env and soluble HTLV-1 and -2 truncated amino terminal SU subdomains. Results Using these SU constructs, we found that the 183 and 178 amino terminal residues of the HTLV-1 and -2 Env, respectively, were sufficient to efficiently bind target cells of different species. Binding resulted from bona fide interaction with the HTLV receptor as isolated SU subdomains specifically interfered with HTLV Env-mediated binding, cell fusion, and cell-free as well as cell-to-cell infection. Therefore, the HTLV receptor-binding domain (RBD) lies in the amino terminus of the SU, immediately upstream of a central immunodominant proline rich region (Env residues 180 to 205), that we show to be dispensible for receptor-binding and interference. Moreover, we identified a highly conserved tyrosine residue at position 114 of HTLV-1 Env, Tyr114, as critical for receptor-binding and subsequent interference to cell-to-cell fusion and infection. Finally, we observed that residues in the vicinity of Tyr114 have lesser impact on receptor binding and had various efficiency in interference to post-binding events. Conclusions The first 160 residues of the HTLV-1 and -2 mature cleaved SU fold as autonomous domains that contain all the determinants required for binding the HTLV receptor.
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- 2004
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23. Haploinsufficiency of the Primary Familial Brain Calcification Gene SLC20A2 Mediated by Disruption of a Regulatory Element.
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Cassinari, Kévin, Rovelet‐Lecrux, Anne, Tury, Sandrine, Quenez, Olivier, Richard, Anne‐Claire, Charbonnier, Camille, Olaso, Robert, Boland, Anne, Deleuze, Jean‐François, Besancenot, Jean‐François, Delpont, Benoit, Pouliquen, Dorothée, Lecoquierre, François, Chambon, Pascal, Thauvin‐Robinet, Christel, Campion, Dominique, Frebourg, Thierry, Battini, Jean‐Luc, Nicolas, Gaël, and Rovelet-Lecrux, Anne
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BRAIN metabolism ,RESEARCH ,BRAIN diseases ,GENETIC mutation ,GENETICS ,RESEARCH methodology ,MEDICAL cooperation ,EVALUATION research ,COMPARATIVE studies ,RESEARCH funding ,EPITHELIAL cells ,CARRIER proteins - Abstract
Objective: Primary familial brain calcification (PFBC) is a rare cerebral microvascular calcifying disorder with diverse neuropsychiatric expression. Five genes were reported as PFBC causative when carrying pathogenic variants. Haploinsufficiency of SLC20A2, which encodes an inorganic phosphate importer, is a major cause of autosomal-dominant PFBC. However, PFBC remains genetically unexplained in a proportion of patients, suggesting the existence of additional genes or cryptic mutations. We analyzed exome sequencing data of 71 unrelated, genetically unexplained PFBC patients with the aim to detect copy number variations that may disrupt the expression of core PFBC-causing genes.Methods: After the identification of a deletion upstream of SLC20A2, we assessed its consequences on gene function by reverse transcriptase droplet digital polymerase chain reaction (RT-ddPCR), an ex vivo inorganic phosphate uptake assay, and introduced the deletion of a putative SLC20A2 enhancer mapping to this region in human embryonic kidney 293 (HEK293) cells by clustered regularly interspaced short palindromic repeats (CRISPR) - CRISPR-associated protein 9 (Cas9).Results: The 8p11.21 deletion, segregating with PFBC in a family, mapped 35 kb upstream of SLC20A2. The deletion carriers/normal controls ratio of relative SLC20A2 mRNA levels was 60.2% (P < 0.001). This was comparable with that of patients carrying an SLC20A2 premature stop codon (63.4%; P < 0.001). The proband exhibited a 39.3% decrease of inorganic phosphate uptake in blood (P = 0.015). In HEK293 cells, we observed a 39.8% decrease in relative SLC20A2 mRNA levels after normalization on DNA copy number (P < 0.001).Discussion: We identified a deletion of an enhancer of SLC20A2 expression, with carriers showing haploinsufficiency in similar ranges to loss-of-function alleles, and we observed reduced mRNA levels after deleting this element in a cellular model. We propose a 3-step strategy to identify and easily assess the effect of such events. © 2020 International Parkinson and Movement Disorder Society. [ABSTRACT FROM AUTHOR]- Published
- 2020
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24. The ubiquitous glucose transporter GLUT-1 is a receptor for HTLV
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Manel, Nicolas, Kim, Felix J., Kinet, Sandrina, Taylor, Naomi, Sitbon, Marc, and Battini, Jean-Luc
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Biological transport -- Physiological aspects ,Cell receptors ,Carrier proteins -- Physiological aspects ,HTLV-I (Virus) -- Physiological aspects ,Biological sciences - Abstract
Research demonstrates that the vertebrate glucose transporter, GLUT-1, is a receptor for HTLV and the receptor binding domains of both HTLV-1 and -2 envelope glycoproteins inhibit glucose transport by interacting with GLUT-1. Data indicate that inhibition of glucose transport or GLUT-1 expression blocks receptor binding and HTLV envelope-driven infection.
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- 2003
25. GLUT-1 is the receptor of retrovirus HTLV
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Manel, N., Kinet, S., Kim, F. J., Taylor, N., Sitbon, Marc, Battini, Jean-Luc, Institut de Génétique Moléculaire de Montpellier (IGMM), and Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)
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[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,virus - Published
- 2004
26. A new retroelement constituted by a natural alternatively spliced RNA of murine replication-competent retroviruses (vol 22, pg 4866, 2003)
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Houzet, L., Battini, Jean-Luc, Bernard, E., Thibert, V., Mougel, M. N., Institut de Génétique Moléculaire de Montpellier (IGMM), and Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)
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[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology - Published
- 2003
27. Cytostatic Effect of Repeated Exposure to Simvastatin: A Mechanism for Chronic Myotoxicity Revealed by the Use of Mesodermal Progenitors Derived from Human Pluripotent Stem Cells.
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Peric, Delphine, Egesipe, Anne-Laure, Pinset, Christian, Peschanski, Marc, Barragan, Isabel, Ingelman-Sundberg, Magnus, Giraud-Triboult, Karine, Laustriat, Delphine, Meyniel-Schicklin, Laurène, Lotteau, Vincent, Cousin, Christelle, Petit, Vincent, Touhami, Jawida, Battini, Jean-Luc, and Sitbon, Marc
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PLURIPOTENT stem cells ,MESODERM ,SIMVASTATIN - Abstract
Statin treatment of hypercholesterolemia can lead to chronic myotoxicity which is, in most cases, alleviated by drug withdrawal. Cellular and molecular mechanisms of this adverse effect have been elusive, in particular because of the lack of in vitro models suitable for long-term exposures. We have taken advantage of the properties of human pluripotent stem cell-derived mesodermal precursors, that can be maintained unaltered in vitro for a long period of time, to develop a model of repeated exposures to simvastatin during more than 2 weeks. This approach unveiled major differences, both in functional and molecular terms, in response to single versus repeated-dose exposures to simvastatin. The main functional effect of the in vitro simvastatin-induced long-term toxicity was a loss of proliferative capacity in the absence of concomitant cell death, revealing that cytostatic effect could be a major contributor to statin-induced myotoxicity. Comparative analysis of molecular modifications induced by simvastatin short-term versus prolonged exposures demonstrated powerful adaptive cell responses, as illustrated by the dramatic decrease in the number of differentially expressed genes, distinct biological pathway enrichments, and distinct patterns of nutrient transporters expressed at the cell surface. This study underlines the potential of derivatives of human pluripotent stem cells for developing new approaches in toxicology, in particular for chronic toxicity testing. S tem C ells 2015;33:2936-2948 [ABSTRACT FROM AUTHOR]
- Published
- 2015
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28. Heterogeneous susceptibility of circulating SIV isolate capsids to HIV-interacting factors.
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Mamede, João I, Sitbon, Marc, Battini, Jean-Luc, and Courgnaud, Valérie
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DISEASE susceptibility ,SIMIAN immunodeficiency virus ,CAPSIDS ,HIV ,CYCLOPHILINS ,IMMUNOSUPPRESSION - Abstract
Background: Many species of non-human primates in Africa are naturally infected by simian immunodeficiency viruses (SIV) and humans stand at the forefront of exposure to these viruses in Sub-Saharan Africa. Cross-species transmission and adaptation of SIV to humans have given rise to human immunodeficiency viruses (HIV-1 and HIV-2) on twelve accountable, independent occasions. However, the determinants contributing to a simian-to-human lasting transmission are not fully understood. Following entry, viral cores are released into the cytoplasm and become the principal target of host cellular factors. Here, we evaluated cellular factors likely to be involved in potential new SIV cross-species transmissions. We investigated the interactions of capsids from naturally circulating SIV isolates with both HIV-1 restricting (i.e. TRIM5 proteins) and facilitating (i.e. cyclophilin A and nucleopore-associated Nup358/RanBP2 and Nup153) factors in single-round infectivity assays that reproduce early stages of the viral life-cycle. Results: We show that human TRIM5α is unlikely to prevent cross-species transmission of any SIV we tested and observed that the SIV CA-CypA interaction is a widespread but not a universal feature. Moreover, entry in the nucleus of different SIV appeared to follow pathways that do not necessarily recruit Nup358/RanBP2 or Nup153, and this regardless of their interaction with CypA. Nevertheless, we found that, like HIV-1, human-adapted HIV-2 infection was dependent on Nup358/RanBP2 and Nup153 interactions for optimal infection. Furthermore, we found that, unlike HIV CA, SIV CA did not require a direct interaction with the Cyp-like domain of Nup358/RanBP2 to carry out successful infection. Conclusions: Circulating SIV present a variety of phenotypes with regard to CA-interacting restricting or facilitating factors. Altogether, we unveiled unidentified pathways for SIV CA, which could also be exploited by HIV in different cellular contexts, to drive entry into the nucleus. Our findings warrant a closer evaluation of other potential defenses against circulating SIV. [ABSTRACT FROM AUTHOR]
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- 2013
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29. Inorganic Phosphate Export by the Retrovirus Receptor XPR1 in Metazoans.
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Giovannini, Donatella, Touhami, Jawida, Charnet, Pierre, Sitbon, Marc, and Battini, Jean-Luc
- Abstract
Summary: Inorganic phosphate uptake is a universal function accomplished by transporters that are present across the living world. In contrast, no phosphate exporter has ever been identified in metazoans. Here, we show that depletion of XPR1, a multipass membrane molecule initially identified as the cell-surface receptor for xenotropic and polytropic murine leukemia retroviruses (X- and P-MLV), induced a decrease in phosphate export and that reintroduction of various XPR1 proteins, from fruit fly to human, rescued this defect. Inhibition of phosphate export was also obtained with a soluble ligand generated from the envelope-receptor-binding domain of X-MLV in all human cell lines tested, as well as in diverse stem cells and epithelial cells derived from renal proximal tubules, the main site of phosphate homeostasis regulation. These results provide new insights on phosphate export in metazoans and the role of Xpr1 in this function. [Copyright &y& Elsevier]
- Published
- 2013
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30. Glut1-mediated glucose transport regulates HIV infection.
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Séverine Loisel-Meyer, Swainson, Louise, Craveiro, Marco, Oburoglu, Leal, Mongellaz, Cedric, Costa, Caroline, Martinez, Marion, Cosset, François-Loic, Battini, Jean-Luc, Herzenberg, Leonard A., Herzenberg, Leonore A., Atkuri, Kondala R., Sitbon, Marc, Kinet, Sandrina, Verhoeyen, Els, and TayIor, Naomi
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GLUCOSE transporters ,HIV infections ,CELL cycle ,T cells ,CYTOKINES - Abstract
Cell cycle entry is commonly considered to positively regulate HIV-1 infection of CD4 T cells, raising the question as to how quiescent lymphocytes, representing a large portion of the viral reservoir, are infected in vivo. Factors such as the homeostatic cytokine IL-7 have been shown to render quiescent T cells permissive to HIV-1 infection, presumably by transiently stimulating their entry into the cell cycle. However, we show here that at physiological oxygen (O
2 ) levels (2-5% O2 tension in lymphoid organs), IL-7 stimulation generates an environment permissive to HIV-1 infection, despite a significantly attenuated level of cell cycle entry. We identify the IL-7-induced increase in Glut1 expression, resulting in augmented glucose uptake, as a key factor in rendering these T lymphocytes susceptible to HIV-1 infection. HIV-1 infection of human T cells is abrogated either by impairment of Glut1 signal transduction or by siRNA-mediated Glut1 down-regulation. Consistent with this, we show that the susceptibility of human thymocyte subsets to HIV-1 infection correlates with Glut1 expression; single-round infection is markedly higher in the Glut1-expressing double-positive thymocyte population than in any of the Glut1-negative subsets. Thus, our studies reveal the Glut1-mediated metabolic pathway as a critical regulator of HIV-1 infection in human CD4 T cells and thymocytes. [ABSTRACT FROM AUTHOR]- Published
- 2012
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31. Regional characterization of energy metabolism in the brain of normal and MPTP-intoxicated mice using new markers of glucose and phosphate transport.
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Lagrue, Emmanuelle, Abe, Hiroyuki, Lavanya, Madakasira, Touhami, Jawida, Bodard, Sylvie, Chalon, Sylvie, Battini, Jean-Luc, Sitbon, Marc, and Castelnau, Pierre
- Subjects
RETROVIRUSES ,HOST-virus relationships ,ENERGY metabolism ,HTLV ,GLYCOPROTEINS - Abstract
The gibbon ape leukemia virus (GALV), the amphotropic murine leukemia virus (AMLV) and the human T-cell leukemia virus (HTLV) are retroviruses that specifically bind nutrient transporters with their envelope glycoproteins (Env) when entering host cells. Here, we used tagged ligands derived from GALV, AMLV, and HTLV Env to monitor the distribution of their cognate receptors, the inorganic phosphate transporters PiT1 and PiT2, and the glucose transporter GLUT1, respectively, in basal conditions and after acute energy deficiency. For this purpose, we monitored changes in the distribution of PiT1, PiT2 and GLUT1 in the cerebellum, the frontal cortex, the corpus callosum, the striatum and the substantia nigra (SN) of C57/BL6 mice after administration of 1-methyl-4-phenyl-1,2,3,6 tetrahydropyridinium (MPTP), a mitochondrial complex I inhibitor which induces neuronal degeneration in the striato-nigral network. The PiT1 ligand stained oligodendrocytes in the corpus callosum and showed a reticular pattern in the SN. The PiT2 ligand stained particularly the cerebellar Purkinje cells, while GLUT1 labelling was mainly observed throughout the cortex, basal ganglia and cerebellar gray matter. Interestingly, unlike GLUT1 and PiT2 distributions which did not appear to be modified by MPTP intoxication, PiT1 immunostaining seemed to be more extended in the SN. The plausible reasons for this change following acute energy stress are discussed. These new ligands therefore constitute new metabolic markers which should help to unravel cellular adaptations to a wide variety of normal and pathologic conditions and to determine the role of specific nutrient transporters in tissue homeostasis. [ABSTRACT FROM AUTHOR]
- Published
- 2010
32. Isolated receptor binding domains of HTLV-1 and HTLV-2 envelopes bind Glut-1 on activated CD4+ and CD8+ T cells.
- Author
-
Kinet, Sandrina, Swainson, Louise, Lavanya, Madakasira, Mongellaz, Cedric, Montel-Hagen, Amélie, Craveiro, Marco, Manel, Nicolas, Battini, Jean-Luc, Sitbon, Marc, and Taylor, Naomi
- Subjects
HTLV-I ,HTLV ,VIRAL envelopes ,T cells ,GLYCOPROTEINS ,LYMPHOCYTES ,VIROLOGY - Abstract
Background: We previously identified the glucose transporter Glut-1, a member of the multimembrane-spanning facilitative nutrient transporter family, as a receptor for both HTLV-1 and HTLV-2. However, a recent report concluded that Glut-1 cannot serve as a receptor for HTLV-1 on CD4 T cells: This was based mainly on their inability to detect Glut-1 on this lymphocyte subset using the commercial antibody mAb1418. It was therefore of significant interest to thoroughly assess Glut-1 expression on CD4 and CD8 T cells, and its association with HTLV-1 and -2 envelope binding. Results: As previously reported, ectopic expression of Glut-1 but not Glut-3 resulted in significantly augmented binding of tagged proteins harboring the receptor binding domains of either HTLV-1 or HTLV-2 envelope glycoproteins (H1
RBD or H2RBD ). Using antibodies raised against the carboxy-terminal peptide of Glut-1, we found that Glut-1 expression was significantly increased in both CD4 and CD8 cells following TCR stimulation. Corresponding increases in the binding of H1RBD as well as H2RBD , not detected on quiescent T cells, were observed following TCR engagement. Furthermore, increased Glut-1 expression was accompanied by a massive augmentation in glucose uptake in TCR-stimulated CD4 and CD8 lymphocytes. Finally, we determined that the apparent contradictory results obtained by Takenouchi et al were due to their monitoring of Glut-1 with a mAb that does not bind cells expressing endogenous Glut-1, including human erythrocytes that harbor 300,000 copies per cell. Conclusion: Transfection of Glut-1 directly correlates with the capacities of HTLV-1 and HTLV-2 envelope-derived ligands to bind cells. Moreover, Glut-1 is induced by TCR engagement, resulting in massive increases in glucose uptake and binding of HTLV-1 and -2 envelopes to both CD4 and CD8 T lymphocytes. Therefore, Glut-1 is a primary binding receptor for HTLV-1 and HTLV-2 envelopes on activated CD4 as well as CD8 lymphocytes. [ABSTRACT FROM AUTHOR]- Published
- 2007
- Full Text
- View/download PDF
33. Glucose transporter 1 expression identifies a population of cycling CD4+CD8+ human thymocytes with high CXCR4-induced chemotaxis.
- Author
-
Swainson, Louise, Kinet, Sandrina, Manel, Nicolas, Battini, Jean-Luc, Sitbon, Marc, and Taylor, Naomi
- Subjects
T cell receptors ,CELL membranes ,BLOOD proteins ,CARRIER proteins ,IRON in the body ,LYMPHOCYTES - Abstract
GLUT1, the major glucose transporter in peripheral I lymphocytes, is induced upon T cell receptor activation. However, the role of GLUT1 during human thymocyte differentiation remains to be evaluated. Our identification of GLUT1 as the human T lymphotrophic virus (HTLV) receptor has enabled us to use tagged HTLV-receptor-binding domain fusion proteins to specifically monitor surface GLUT1 expression. Here, we identify a unique subset of CD4
+ CD8+ double-positive (DP) thymocytes, based on their GLUT1 surface expression. Whereas these cells express variable levels of CD8, they express uniformly high levels of CD4. Glucose uptake was 7-fold higher in CD4hi DP thymocytes than in CD4lo DP thymocytes (P = 0.0002). Further analyses indicated that these GLUT1+ thymocytes are early post-β-selection, as demonstrated by low levels of T cell receptor (TCR)αβ and CD3. This population of immature GLUT1+ DP cells is rapidly cycling and can be further distinguished by specific expression of the transferrin receptor. Importantly, the CXCR4 chemokine receptor is expressed at 15-fold higher levels on GLUT1+ DP thymocytes, as compared with the DP GLUT1- subset and the former cells show enhanced chemotaxis to the CXCR4 ligand CXCL12. Thus, during human thymopoiesis, GLUT1 is up-regulated after β-selection, and these immature DP cells constitute a population with distinct metabolic and chemotactic properties. [ABSTRACT FROM AUTHOR]- Published
- 2005
- Full Text
- View/download PDF
34. Human T Cell Leukemia Virus Envelope Binding and Virus Entry Are Mediated by Distinct Domains of the Glucose Transporter GLUT1.
- Author
-
Manel, Nicolas, Battini, Jean-Luc, and Sitbon, Marc
- Subjects
- *
HTLV , *HTLV-I , *GLUCOSE , *PROTEIN binding , *EXTRACELLULAR matrix , *T cells - Abstract
The glucose transporter GLUT1, a member of the multimembrane-spanning facilitative nutrient transporter family, serves as a receptor for human T cell leukemia virus (HTLV) infection. Here, we show that the 7 amino acids of the extracellular loop 6 of GLUT1 (ECL6) placed in the context of the related GLUT3 transporter were sufficient for HTLV envelope binding. Glutamate residue 426 in ECL6 was identified as critical for binding. However, binding to ECL6 was not sufficient for HTLV envelope-driven infection. Infection required two additional determinants located in ECL1 and ECL5, which otherwise did not influence HTLV envelope binding. Moreover the single N-glycosylation chain located in ECL1 was not required for HTLV infection. Therefore, binding involves a discrete determinant in the carboxyl terminal ECL6, whereas post-binding events engage extracellular sequences in the amino and carboxyl terminus of GLUT1. [ABSTRACT FROM AUTHOR]
- Published
- 2005
- Full Text
- View/download PDF
35. Emergence of vertebrate retroviruses and envelope capture
- Author
-
Kim, Felix J., Battini, Jean-Luc, Manel, Nicolas, and Sitbon, Marc
- Subjects
- *
RETROVIRUS diseases , *GENETICS , *LEUKEMIA - Abstract
Retroviruses are members of the superfamily of retroelements, mobile genetic elements that transpose via an RNA intermediate. However, retroviruses are distinct from other retroelements in that their “transposition” is not confined to single cells but extends to neighboring cells and organisms. As such, the “transposition” of these elements is defined as infection. It appears that a key step in the conversion of a retrotransposon into a retrovirus is the modular acquisition or capture of an envelope glycoprotein (Env) which facilitates dissemination from its initial host cell. Here we present several examples of retroviruses for which envelope capture has been identified. Indeed, capture may explain the notable conservation of env sequences among otherwise phylogenetically distant retroviruses. In a recent example, sequence homologies reported between the env of the phylogenetically distant murine leukemia viruses (MLV) and human T cell leukemia viruses (HTLV) argue in favor of an env capture by the latter. Env acquisition can provide new adaptive properties to replication-competent viruses in addition to altering their host range. Also, the captured env can alter the spectrum of physiological affects of infection in new host cells and organisms. The elucidation of such envelope exchanges and properties thereof should contribute significantly to the clarification of retroviral phylogeny, insight into retroviral pathogenesis, and to the discovery of new retroviruses. [Copyright &y& Elsevier]
- Published
- 2004
- Full Text
- View/download PDF
36. HTLV-1 and -2 envelope SU subdomains and critical determinants in receptor binding.
- Author
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Kim, Felix J., Manel, Nicolas, Garrido, Edith N., Valle, Carine, Sitbon, Marc, and Battini, Jean-Luc
- Subjects
HTLV ,HTLV-I ,GLYCOPROTEINS ,VIRAL proteins ,CELL receptors - Abstract
Background: Human T-cell leukemia virus (HTLV) -1 and -2 are deltaretroviruses that infect a wide range of cells. Glut1, the major vertebrate glucose transporter, has been shown to be the HTLV Env receptor. While it is well established that the extracellular surface component (SU) of the HTLV envelope glycoprotein (Env) harbors all of the determinants of interaction with the receptor, identification of SU subdomains that are necessary and sufficient for interaction with the receptor, as well as critical amino acids therein, remain to be precisely defined. Although highly divergent in the rest of their genomes, HTLV and murine leukemia virus (MLV) Env appear to be related and based on homologous motifs between the HTLV and MLV SU, we derived chimeric HTLV/MLV Env and soluble HTLV-1 and -2 truncated amino terminal SU subdomains. Results: Using these SU constructs, we found that the 183 and 178 amino terminal residues of the HTLV-1 and -2 Env, respectively, were sufficient to efficiently bind target cells of different species. Binding resulted from bona fide interaction with the HTLV receptor as isolated SU subdomains specifically interfered with HTLV Env-mediated binding, cell fusion, and cell-free as well as cell-to-cell infection. Therefore, the HTLV receptor-binding domain (RBD) lies in the amino terminus of the SU, immediately upstream of a central immunodominant proline rich region (Env residues 180 to 205), that we show to be dispensible for receptor-binding and interference. Moreover, we identified a highly conserved tyrosine residue at position
114 of HTLV-1 Env, Tyr114 , as critical for receptor-binding and subsequent interference to cell-to-cell fusion and infection. Finally, we observed that residues in the vicinity of Tyr114 have lesser impact on receptor binding and had various efficiency in interference to post-binding events. Conclusions: The first 160 residues of the HTLV-1 and -2 mature cleaved SU fold as autonomous domains that contain all the determinants required for binding the HTLV receptor. [ABSTRACT FROM AUTHOR]- Published
- 2004
- Full Text
- View/download PDF
37. Mutations in XPR1 cause primary familial brain calcification associated with altered phosphate export.
- Author
-
Legati, Andrea, Sears, Renee L, Ramos, Eliana Marisa, Lang, Anthony E, Miedzybrodzka, Zosia, Simpson, Sheila A, Paucar, Martin, Svenningsson, Per, Paulson, Henry, Pariente, Jérémie, Richard, Anne-Claire, Salins, Naomi S, Striano, Pasquale, Unni, Vivek K, Vanakker, Olivier, Giovannini, Donatella, López-Sánchez, Uriel, Sitbon, Marc, Battini, Jean-Luc, and Wessels, Marja W
- Subjects
CALCIFICATION ,NEUROLOGICAL disorders ,CALCIUM phosphate ,EXONS (Genetics) ,HOMEOSTASIS - Abstract
Primary familial brain calcification (PFBC) is a neurological disease characterized by calcium phosphate deposits in the basal ganglia and other brain regions and has thus far been associated with SLC20A2, PDGFB or PDGFRB mutations. We identified in multiple families with PFBC mutations in XPR1, a gene encoding a retroviral receptor with phosphate export function. These mutations alter phosphate export, implicating XPR1 and phosphate homeostasis in PFBC. [ABSTRACT FROM AUTHOR]
- Published
- 2015
- Full Text
- View/download PDF
38. The RD114/simian type D retrovirus receptor is a neural amino acid transporter.
- Author
-
Rasko, John E.J. and Battini, Jean-Luc
- Subjects
- *
RETROVIRUSES , *AMINO acids , *RETROVIRUS diseases , *PHYSIOLOGY , *GENETICS - Abstract
Characterizes the common cell-surface receptor of the RD114/simian type D retroviruses. Use of retroviral cDNA library approach; Transfer and expression of cDNA; Cloning of neutral amino acid transporter; Impairment of amino acid transport due to infection of cells with retroviruses.
- Published
- 1999
- Full Text
- View/download PDF
39. Induction of GLUT1 during Erythropoiesis Triggers a Switch from Glucose to DHA Uptake in Vitamin C-Defective Mammals.
- Author
-
Montel-Hagen, Amelie, Kinet, Sandrina, Manel, Nicolas, Mongellaz, Cedric, Prohaska, Rainer, Battini, Jean-Luc, Delaunay, Jean, Sitbon, Marc, and Taylor, Naomi
- Published
- 2007
- Full Text
- View/download PDF
40. Identification of Copper Transporter 1 as a Receptor for Feline Endogenous Retrovirus ERV-DC14.
- Author
-
Tury, Sandrine, Giovannini, Donatella, Ivanova, Svilena, Touhami, Jawida, Courgnaud, Valérie, and Battini, Jean-Luc
- Subjects
- *
VIRAL tropism , *FELINE leukemia virus , *COPPER , *CELL receptors , *GENETIC testing , *CATS - Abstract
Vertebrates harbor hundreds of endogenous retroviral (ERV) sequences in their genomes, which are considered signs of past infections that occurred during evolution. On rare occasions, ERV genes like env are maintained and coopted by hosts for physiological functions, but they also participate in recombination events with exogenous retroviruses to generate rearranged viruses with novel tropisms. In domestic cats, feline leukemia virus type D (FeLV-D) has been described as a recombinant virus between the infectious FeLV-A and likely the ERV-DC14 env gene that resulted in an extended tropism due to the usage of a new uncharacterized retroviral receptor. Here, we report the identification of SLC31A1 encoding the copper transporter 1 (CTR1) as a susceptibility gene for ERV-DC14 infection. Expression of human CTR1 into nonpermissive cells was sufficient to confer sensitivity to ERV-DC14 pseudotype infection and to increase the binding of an ERV-DC14 Env ligand. Moreover, inactivation of CTR1 by genome editing or cell surface downmodulation of CTR1 by a high dose of copper dramatically decreased ERV-DC14 infection and binding, while magnesium treatment had no effect. We also investigated the role of CTR1 in the nonpermissivity of feline and hamster cells. While feline CTR1 was fully functional for ERV-DC14, we found that binding was strongly reduced upon treatment with conditioned medium of feline cells, suggesting that the observed resistance to infection was a consequence of CTR1 saturation. In contrast, hamster CTR1 was inactive due to the presence of a N-linked glycosylation site at position 27, which is absent in the human ortholog. These results provide evidence that CTR1 is a receptor for ERV-DC14. Along with chimpanzee endogenous retrovirus type 2, ERV-DC14 is the second family of endogenous retrovirus known to have used CTR1 during past infections of vertebrates. IMPORTANCE Receptor usage is an important determinant of diseases induced by pathogenic retroviruses. In the case of feline leukemia viruses, three subgroups (A, B, and C) based on their ability to recognize different cell host receptors, respectively, the thiamine transporter THTR1, the phosphate transporter PiT1, and the heme exporter FLVCR1, are associated with distinct feline diseases. FeLV-A is horizontally transmitted and found in all naturally infected cats, while FeLV-B and FeLV-C have emerged from FeLV-A, respectively, by recombination with endogenous retroviral env sequences or by mutations in the FeLV-A env gene, both leading to a switch in receptor usage and in subsequent in vivo tropism. Here, we set up a genetic screen to identify the retroviral receptor of ERV-DC14, a feline endogenous provirus whose env gene has been captured by infectious FeLV-A to give rise to FeLV-D in a process similar to FeLV-B. Our results reveal that the copper transporter CTR1 was such a receptor and provide new insights into the acquisition of an expanded tropism by FeLV-D. [ABSTRACT FROM AUTHOR]
- Published
- 2022
- Full Text
- View/download PDF
41. Residues in the Murine Leukemia Virus Capsid That Differentially Govern Resistance to Mouse Fv1 and Human Ref1 Restrictions.
- Author
-
Lassaux, Adeline, Sitbon, Marc, and Battini, Jean-Luc
- Subjects
- *
MOUSE leukemia viruses , *LEUKEMIA , *VIRUSES , *GENES , *RETROVIRUSES - Abstract
We identified new residues within a 101-amino-acid stretch of the murine leukemia virus capsid that differentially modulate resistance and susceptibility to the mouse Fv1 and human Ref1 genes. Among these residues, aspartate 92 and histidine 117 are both required for Fv1b resistance, whereas the latter is sufficient to confer Ref1 resistance. [ABSTRACT FROM AUTHOR]
- Published
- 2005
- Full Text
- View/download PDF
42. Interplay between primary familial brain calcificationassociated SLC20A2 and XPR1 phosphate transporters requires inositol polyphosphates for control of cellular phosphate homeostasis.
- Author
-
López-Sánchez, Uriel, Tury, Sandrine, Nicolas, Gaël, Wilson, Miranda S., Jurici, Snejana, Ayrignac, Xavier, Courgnaud, Valérie, Saiardi, Adolfo, Sitbon, Marc, and Battini, Jean-Luc
- Subjects
- *
INOSITOL phosphates , *PHOSPHATES , *POLYPHOSPHATES , *GENE silencing , *HOMEOSTASIS , *GENETIC disorders , *SYMPTOMS - Abstract
Solute carrier family 20 member 2 (SLC20A2) and xenotropic and polytropic retrovirus receptor 1 (XPR1) are transporters with phosphate uptake and efflux functions, respectively. Both are associated with primary familial brain calcification (PFBC), a genetic disease characterized by cerebral calciumphosphate deposition and associated with neuropsychiatric symptoms. The association of the two transporters with the same disease suggests that they jointly regulate phosphate fluxes and cellular homeostasis, but direct evidence is missing. Here, we found that cross-talk between SLC20A2 and XPR1 regulates phosphate homeostasis, and we identified XPR1 as a key inositol polyphosphate (IP)-dependent regulator of this process. We found that overexpression of WT SLC20A2 increased phosphate uptake, as expected, but also unexpectedly increased phosphate efflux, whereas PFBCassociated SLC20A2 variants did not. Conversely, SLC20A2 depletion decreased phosphate uptake only slightly, most likely compensated for by the related SLC20A1 transporter, but strongly decreased XPR1-mediated phosphate efflux. The SLC20A2-XPR1 axis maintained constant intracellular phosphate and ATP levels, which both increased in XPR1 KO cells. Elevated ATP levels are a hallmark of altered inositol pyrophosphate (PP-IP) synthesis, and basal ATP levels were restored after phosphate efflux rescue with WT XPR1 but not with XPR1 harboring a mutated PP-IP–binding pocket. Accordingly, inositol hexakisphosphate kinase 1-2 (IP6K1-2) gene inactivation or IP6K inhibitor treatment abolished XPR1-mediated phosphate efflux regulation and homeostasis. Our findings unveil an SLC20A2-XPR1 interplay that depends on IPs such as PP-IPs and controls cellular phosphate homeostasis via the efflux route, and alteration of this interplay likely contributes to PFBC [ABSTRACT FROM AUTHOR]
- Published
- 2020
- Full Text
- View/download PDF
43. Role of N-linked Glycosylation in the Activity of the Friend Murine Leukemia Virus SU Protein Receptor-Binding Domain
- Author
-
Battini, Jean-Luc, Kayman, Samuel C., Pinter, Abraham, Heard, Jean Michel, and Danos, Olivier
- Published
- 1994
- Full Text
- View/download PDF
44. Metabolic Adaptation of Neutrophils in Cystic Fibrosis Airways Involves Distinct Shifts in Nutrient Transporter Expression.
- Author
-
Laval, Julie, Touhami, Jawida, Herzenberg, Leonore A., Conrad, Carol, Taylor, Naomi, Battini, Jean-Luc, Sitbon, Marc, and Tirouvanziam, Rabindra
- Subjects
- *
CYSTIC fibrosis , *NEUTROPHILS , *CELL metabolism , *AIRWAY (Anatomy) , *EXOCYTOSIS , *PROTEIN expression - Abstract
Inflammatory conditions can profoundly alter human neutrophils, a leukocyte subset generally viewed as terminally differentiated and catabolic. In cystic fibrosis (CF) patients, neutrophils recruited to CF airways show active exocytosis and sustained phosphorylation of prosurvival, metabolic pathways. Because the CF airway lumen is also characterized by high levels of free glucose and amino acids, we compared surface expression of Glut1 (glucose) and ASCT2 (neutral amino acids) transporters, as well as that of PiT1 and PiT2 (inorganic phosphate transporters), in blood and airway neutrophils, using specific retroviral envelope-derived ligands. Neither nutrient transporter expression nor glucose uptake was altered on blood neutrophils from CF patients compared with healthy controls. Notably, however, airway neutrophils of CF patients had higher levels of PiT1 and Glut1 and increased glucose uptake compared with their blood counterparts. Based on primary granule exocytosis and scatter profiles, CF airway neutrophils could be divided into two subsets, with one of the subsets characterized by more salient increases in Glut1, ASCT2, PiT1, and PiT2 expression. Moreover, in vitro exocytosis assays of blood neutrophils suggest that surface nutrient transporter expression is not directly associated with primary (or secondary) granule exocytosis. Although expression of nutrient transporters on CF blood or airway neutrophils was not altered by genotype, age, gender, or Pseudomonas aeruginosa infection, oral steroid treatment decreased Glut1 and PiT2 levels in blood neutrophils. Thus, neutrophils recruited from blood into the CF airway lumen display augmented cell surface nutrient transporter expression and glucose uptake, consistent with metabolic adaptation. [ABSTRACT FROM AUTHOR]
- Published
- 2013
- Full Text
- View/download PDF
45. Erythrocyte Glut1 Triggers Dehydroascorbic Acid Uptake in Mammals Unable to Synthesize Vitamin C
- Author
-
Montel-Hagen, Amélie, Kinet, Sandrina, Manel, Nicolas, Mongellaz, Cédric, Prohaska, Rainer, Battini, Jean-Luc, Delaunay, Jean, Sitbon, Marc, and Taylor, Naomi
- Subjects
- *
ERYTHROCYTES , *GLUCOSE , *ERYTHROPOIESIS , *VITAMIN C - Abstract
Summary: Of all cells, human erythrocytes express the highest level of the Glut1 glucose transporter. However, the regulation and function of Glut1 during erythropoiesis are not known. Here, we report that glucose transport actually decreases during human erythropoiesis despite a >3-log increase in Glut1 transcripts. In contrast, Glut1-mediated transport of L-dehydroascorbic acid (DHA), an oxidized form of ascorbic acid (AA), is dramatically enhanced. We identified stomatin, an integral erythrocyte membrane protein, as regulating the switch from glucose to DHA transport. Notably though, we found that erythrocyte Glut1 and associated DHA uptake are unique traits of humans and the few other mammals that have lost the ability to synthesize AA from glucose. Accordingly, we show that mice, a species capable of synthesizing AA, express Glut4 but not Glut1 in mature erythrocytes. Thus, erythrocyte-specific coexpression of Glut1 with stomatin constitutes a compensatory mechanism in mammals that are unable to synthesize vitamin C. [Copyright &y& Elsevier]
- Published
- 2008
- Full Text
- View/download PDF
46. Human T-Cell Leukemia Virus Type 1 Envelope-Mediated Syncytium Formation Can Be Activated in Resistant Mammalian Cell Lines by a Carboxy-Terminal Truncation of the Envelope Cytoplasmic Domain.
- Author
-
Kim, Felix J., Manel, Nicolas, Boublik, Yvan, Battini, Jean-Luc, and Sitbon, Marc
- Subjects
- *
HTLV-I , *GLYCOPROTEINS , *CELL lines - Abstract
Human T-cell leukemia virus (HTLV) envelope (Env) glycoproteins induce fusion, leading to rampant syncytium formation in a broad range of cell lines. Here, we identified murine, hamster, canine, and porcine cell lines that are resistant to HTLV-1 Env-induced syncytium formation. This resistance was not due to the absence of functional receptors for HTLV Env, as these cells were susceptible to infection with HTLV Env-pseudotyped virions. As murine leukemia virus (MLV) Env and HTLV Env present close structural homologies (F. J. Kim, I. Seiliez, C. Denesvre, D. Lavillette, F. L. Cosset, and M. Sitbon, J. Biol. Chem. 275:23417-23420, 2000), and because activation of syncytium formation by MLV Env generally requires cleavage of the R peptide in the cytoplasmic domain of the Env transmembrane (TM) component, we assessed whether truncation of the cytoplasmic domain of HTLV Env would alleviate this resistance. Indeed, in all resistant cell lines, truncation of the last 8 amino acids of the HTLV Env cytoplasmic domain (HDC8) was sufficient to overcome resistance to HTLV Env-induced syncytium formation. Furthermore, HdC8-mediated cell-to-cell infection titers varied according to the target cell lines and could be significantly higher than that observed with HTLV Env on HeLa cells. These data indicate that a determinant located within the 8 carboxy terminal cytoplasmic amino acids of TM plays a distinct role in HTLV Env-mediated cell-to-cell infection and syncytium formation. [ABSTRACT FROM AUTHOR]
- Published
- 2003
- Full Text
- View/download PDF
47. Response: Species Diversity in GLUT Expression and Function
- Author
-
Montel-Hagen, Amélie, Kinet, Sandrina, Manel, Nicolas, Mongellaz, Cedric, Prohaska, Rainer, Battini, Jean-Luc, Delaunay, Jean, Sitbon, Marc, and Taylor, Naomi
- Published
- 2009
- Full Text
- View/download PDF
48. Xpr1 Is an Atypical G-Protein-Coupled Receptor That Mediates Xenotropic and Polytropic Murine Retrovirus Neurotoxicity.
- Author
-
Vaughan, Andrew E., Mendoza, Ramon, Aranda, Ramona, Battini, Jean-Luc, and Dusty Miller, A.
- Subjects
- *
NEUROTOXICOLOGY , *G protein coupled receptors - Abstract
An abstract of the article "Xpr1 Is an Atypical G-Protein-Coupled Receptor That Mediates Xenotropic and Polytropic Murine Retrovirus Neurotoxicity," by Andrew E. Vaughan and colleagues is presented.
- Published
- 2012
- Full Text
- View/download PDF
49. Cyclophilins and nucleoporins are required for infection mediated by capsids from circulating HIV-2 primary isolates.
- Author
-
Mamede JI, Damond F, Bernardo A, Matheron S, Descamps D, Battini JL, Sitbon M, and Courgnaud V
- Subjects
- Africa, Western, Animals, Antiviral Restriction Factors, Capsid metabolism, Capsid physiology, Cell Nucleus metabolism, Cell Nucleus virology, HEK293 Cells, HIV Infections metabolism, HIV-1 metabolism, HIV-1 pathogenicity, HIV-2 metabolism, Humans, Mice, Tripartite Motif Proteins, Ubiquitin-Protein Ligases, Virus Replication, Carrier Proteins metabolism, Cyclophilin A metabolism, HIV Infections virology, HIV-2 pathogenicity, Molecular Chaperones metabolism, Nuclear Pore Complex Proteins metabolism
- Abstract
HIV-2 groups have emerged from sooty mangabey SIV and entered the human population in Africa on several separate occasions. Compared to world pandemic HIV-1 that arose from the chimpanzee SIVcpz virus, the SIVsm-derived HIV-2, largely confined to West Africa, is less replicative, less transmissible and less pathogenic. Here, we evaluated the interactions between host cellular factors, which control HIV-1 infection and target the capsid, and HIV-2 capsids obtained from primary isolates from patients with different disease progression status. We showed that, like HIV-1, all HIV-2 CA we tested exhibited a dependence on cyclophilin A. However, we observed no correlation between HIV-2 viremia and susceptibility to hu-TRIM5alpha or dependence to CypA. Finally, we found that all CA from HIV-2 primary isolates exploit Nup358 and Nup153 for nucleus transposition. Altogether, these findings indicate that the ability to use the two latter nucleoporins is essential to infection of human cells for both HIV-1 and HIV-2. This dependence provides another molecular target that could be used for antiviral strategies against both HIV-1 and 2, based on both nucleoporins.
- Published
- 2017
- Full Text
- View/download PDF
50. Glucose and glutamine metabolism regulate human hematopoietic stem cell lineage specification.
- Author
-
Oburoglu L, Tardito S, Fritz V, de Barros SC, Merida P, Craveiro M, Mamede J, Cretenet G, Mongellaz C, An X, Klysz D, Touhami J, Boyer-Clavel M, Battini JL, Dardalhon V, Zimmermann VS, Mohandas N, Gottlieb E, Sitbon M, Kinet S, and Taylor N
- Subjects
- ADP-ribosyl Cyclase 1 metabolism, Animals, Antigens, CD34 metabolism, Biological Transport, Cell Differentiation, Chromatography, Liquid, Erythrocytes cytology, Glycolysis, Green Fluorescent Proteins metabolism, Humans, Mass Spectrometry, Mice, Mice, Inbred C57BL, Minor Histocompatibility Antigens, RNA, Small Interfering metabolism, Amino Acid Transport System ASC metabolism, Cell Lineage, Gene Expression Regulation, Glucose metabolism, Glutamine metabolism, Hematopoietic Stem Cells cytology
- Abstract
The metabolic state of quiescent hematopoietic stem cells (HSCs) is an important regulator of self-renewal, but it is unclear whether or how metabolic parameters contribute to HSC lineage specification and commitment. Here, we show that the commitment of human and murine HSCs to the erythroid lineage is dependent upon glutamine metabolism. HSCs require the ASCT2 glutamine transporter and active glutamine metabolism for erythroid specification. Blocking this pathway diverts EPO-stimulated HSCs to differentiate into myelomonocytic fates, altering in vivo HSC responses and erythroid commitment under stress conditions such as hemolytic anemia. Mechanistically, erythroid specification of HSCs requires glutamine-dependent de novo nucleotide biosynthesis. Exogenous nucleosides rescue erythroid commitment of human HSCs under conditions of limited glutamine catabolism, and glucose-stimulated nucleotide biosynthesis further enhances erythroid specification. Thus, the availability of glutamine and glucose to provide fuel for nucleotide biosynthesis regulates HSC lineage commitment under conditions of metabolic stress., (Copyright © 2014 Elsevier Inc. All rights reserved.)
- Published
- 2014
- Full Text
- View/download PDF
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