P. Pandolfi, F. Grignani, M. Alcalay, A. Mencarelli, A. Biondi et al., Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties, Oncogene, vol.6, pp.1285-1292, 1991.

R. Bernardi and P. Pandolfi, Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies, Nature Reviews Molecular Cell Biology, vol.117, issue.12, pp.1006-1016, 2007.
DOI : 10.1038/nrm2277

V. Lallemand-breitenbach and H. De-thé, PML Nuclear Bodies, Cold Spring Harbor Perspectives in Biology, vol.2, issue.5, p.661, 2010.
DOI : 10.1101/cshperspect.a000661

URL : https://hal.archives-ouvertes.fr/hal-00102123

S. Banani, A. Rice, W. Peeples, Y. Lin, S. Jain et al., Compositional Control of Phase-Separated Cellular Bodies, Cell, vol.166, issue.3, pp.651-663, 2016.
DOI : 10.1016/j.cell.2016.06.010

M. Jeanne, V. Lallemand-breitenbach, O. Ferhi, M. Koken, L. Bras et al., PML/RARA Oxidation and Arsenic Binding Initiate the Antileukemia Response of As2O3, Cancer Cell, vol.18, issue.1, pp.88-98, 2010.
DOI : 10.1016/j.ccr.2010.06.003

URL : https://hal.archives-ouvertes.fr/hal-00652202

H. De-thé and Z. Chen, Acute promyelocytic leukaemia: novel insights into the mechanisms of cure, Nature Reviews Cancer, vol.112, issue.11, pp.775-783, 2010.
DOI : 10.1038/nrc2943

U. Sahin, O. Ferhi, J. M. Benhenda, S. Berthier, C. Jollivet et al., Oxidative stress???induced assembly of PML nuclear bodies controls sumoylation of partner proteins, The Journal of Cell Biology, vol.95, issue.6, pp.931-945, 2014.
DOI : 10.1083/jcb.201305148.dv

URL : https://hal.archives-ouvertes.fr/hal-00992287

S. Tessier, N. Martin-martin, H. De-thé, A. Carracedo, and V. Lallemand-breitenbach, PML, a protein at the cross road of oxidative stress and metabolism, Antioxid Redox Signal, 2016.

U. Sahin, O. Ferhi, X. Carnec, A. Zamborlini, L. Peres et al., Interferon controls SUMO availability via the Lin28 and let-7 axis to impede virus replication, Nature Communications, vol.96, p.4187, 2014.
DOI : 10.1186/gb-2003-5-1-r1

R. Bernardi, A. Papa, and P. Pandolfi, Regulation of apoptosis by PML and the PML-NBs, Oncogene, vol.95, issue.48, pp.6299-6312, 2008.
DOI : 10.1074/jbc.M308302200

M. Geoffroy and R. Hay, An additional role for SUMO in ubiquitin-mediated proteolysis, Nature Reviews Molecular Cell Biology, vol.281, issue.8, pp.564-568, 2009.
DOI : 10.1038/nrm2707

M. Geoffroy and M. Chelbi-alix, Role of Promyelocytic Leukemia Protein in Host Antiviral Defense, Journal of Interferon & Cytokine Research, vol.31, issue.1, pp.145-158, 2011.
DOI : 10.1089/jir.2010.0111

R. Everett, C. Boutell, and B. Hale, Interplay between viruses and host sumoylation pathways, Nature Reviews Microbiology, vol.87, issue.6, pp.400-411, 2013.
DOI : 10.1038/nrmicro3015

P. Cossart, Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes, Proceedings of the National Academy of Sciences, vol.108, issue.49, pp.19484-19491, 2011.
DOI : 10.1073/pnas.1112371108

A. Flotho and F. Melchior, Sumoylation: A Regulatory Protein Modification in Health and Disease, Annual Review of Biochemistry, vol.82, issue.1, pp.357-385, 2013.
DOI : 10.1146/annurev-biochem-061909-093311

D. Ribet, M. Hamon, E. Gouin, M. Nahori, F. Impens et al., Listeria monocytogenes impairs SUMOylation for efficient infection, Nature, vol.22, issue.7292, pp.1192-1195, 2010.
DOI : 10.1038/nature08963

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3627292

F. Impens, L. Radoshevich, P. Cossart, and D. Ribet, Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli, Proceedings of the National Academy of Sciences, vol.111, issue.34, pp.12432-12437, 2014.
DOI : 10.1073/pnas.1413825111

URL : https://hal.archives-ouvertes.fr/pasteur-01104237

S. Sidik, J. Salsman, G. Dellaire, and J. Rohde, Shigella Infection Interferes with SUMOylation and Increases PML-NB Number, PLOS ONE, vol.552, issue.2???3, p.122585, 2015.
DOI : 10.1371/journal.pone.0122585.s002

URL : http://doi.org/10.1371/journal.pone.0122585

S. Fritah, N. Lhocine, F. Golebiowski, J. Mounier, A. Andrieux et al., Sumoylation controls host anti-bacterial response to the gut invasive pathogen Shigella flexneri, EMBO reports, vol.15, issue.9, pp.965-972, 2014.
DOI : 10.15252/embr.201338386

S. Verma, G. Mohapatra, S. Ahmad, R. S. Jain, S. Khalsa et al., Salmonella Engages Host MicroRNAs To Modulate SUMOylation: a New Arsenal for Intracellular Survival, Molecular and Cellular Biology, vol.35, issue.17, pp.2932-294600397, 2015.
DOI : 10.1128/MCB.00397-15

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4525320

A. Decque, O. Joffre, J. Magalhaes, J. Cossec, R. Blecher-gonen et al., Sumoylation coordinates the repression of inflammatory and anti-viral gene-expression programs during innate sensing, Nature Immunology, vol.17, issue.2, pp.140-149, 2015.
DOI : 10.1093/nar/gkq1287

URL : https://hal.archives-ouvertes.fr/pasteur-01380657

T. Kamitani, K. Kito, H. Nguyen, H. Wada, T. Fukuda-kamitani et al., Identification of Three Major Sentrinization Sites in PML, Journal of Biological Chemistry, vol.273, issue.41, pp.26675-26682, 1998.
DOI : 10.1074/jbc.273.41.26675

S. Müller, M. Matunis, and A. Dejean, Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus, The EMBO Journal, vol.17, issue.1, pp.61-70, 1998.
DOI : 10.1093/emboj/17.1.61

A. Ishov, A. Sotnikov, D. Negorev, O. Vladimirova, N. Neff et al., Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1, The Journal of Cell Biology, vol.8, issue.2, pp.221-234, 1999.
DOI : 10.1038/24628

S. Zhong, S. Müller, S. Ronchetti, P. Freemont, A. Dejean et al., Role of SUMO-1-modified PML in nuclear body formation, Blood, vol.95, pp.2748-2752, 2000.

V. Lallemand-breitenbach, J. Zhu, F. Puvion, M. Koken, N. Honoré et al., -Induced Pml or Pml/Retinoic Acid Receptor ?? Degradation, The Journal of Experimental Medicine, vol.73, issue.12, pp.1361-1371, 2001.
DOI : 10.1038/sj.onc.1202366

URL : https://hal.archives-ouvertes.fr/hal-00102123

A. Vertegaal, J. Andersen, S. Ogg, R. Hay, M. Mann et al., Distinct and Overlapping Sets of SUMO-1 and SUMO-2 Target Proteins Revealed by Quantitative Proteomics, Molecular & Cellular Proteomics, vol.5, issue.12, pp.2298-2310, 2006.
DOI : 10.1074/mcp.M600212-MCP200

D. Cuchet-lourenço, C. Boutell, V. Lukashchuk, K. Grant, A. Sykes et al., SUMO Pathway Dependent Recruitment of Cellular Repressors to Herpes Simplex Virus Type 1 Genomes, PLoS Pathogens, vol.139, issue.7, 2011.
DOI : 10.1371/journal.ppat.1002123.s011

F. Galisson, L. Mahrouche, M. Courcelles, E. Bonneil, S. Meloche et al., A Novel Proteomics Approach to Identify SUMOylated Proteins and Their Modification Sites in Human Cells, Molecular & Cellular Proteomics, vol.10, issue.2, 2011.
DOI : 10.1074/mcp.M110.004796

V. Lallemand-breitenbach, J. M. Benhenda, S. Nasr, R. Lei, M. Peres et al., Arsenic degrades PML or PML???RAR?? through a SUMO-triggered RNF4/ubiquitin-mediated pathway, Nature Cell Biology, vol.112, issue.5, pp.547-555, 2008.
DOI : 10.1038/nmeth891

M. Tatham, M. Geoffroy, L. Shen, A. Plechanovova, N. Hattersley et al., RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation, Nature Cell Biology, vol.112, issue.5, pp.538-546, 2008.
DOI : 10.1042/BJ20052030

L. Ivanschitz, Y. Takahashi, F. Jollivet, O. Ayrault, L. Bras et al., PML IV/ARF interaction enhances p53 SUMO-1 conjugation, activation, and senescence, Proceedings of the National Academy of Sciences, vol.112, issue.46, pp.14278-14283, 2015.
DOI : 10.1073/pnas.1507540112

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4655504

A. Lunardi, M. Gaboli, M. Giorgio, R. R. Bygrave, A. Antoniou et al., A Role for PML in Innate Immunity, Genes & Cancer, vol.2, issue.1, pp.10-19, 2011.
DOI : 10.1177/1947601911402682

M. Lecuit, S. Dramsi, C. Gottardi, M. Fedor-chaiken, B. Gumbiner et al., A single amino acid in E-cadherin responsible for host specificity towards the human pathogen Listeria monocytogenes, The EMBO Journal, vol.18, issue.14, pp.3956-3963, 1999.
DOI : 10.1093/emboj/18.14.3956

C. Bécavin, C. Bouchier, P. Lechat, C. Archambaud, S. Creno et al., Comparison of Widely Used Listeria monocytogenes Strains EGD, 10403S, and EGD-e Highlights Genomic Differences Underlying Variations in Pathogenicity, mBio, vol.5, issue.2, pp.969-1400969, 2014.
DOI : 10.1128/mBio.00969-14

M. Lecuit, J. Sonnenburg, P. Cossart, and J. Gordon, Functional Genomic Studies of the Intestinal Response to a Foodborne Enteropathogen in a Humanized Gnotobiotic Mouse Model, Journal of Biological Chemistry, vol.282, issue.20, pp.15065-15072, 2007.
DOI : 10.1074/jbc.M610926200

D. Portnoy, P. Jacks, and D. Hinrichs, Role of hemolysin for the intracellular growth of Listeria monocytogenes, Journal of Experimental Medicine, vol.167, issue.4, pp.1459-1471, 1988.
DOI : 10.1084/jem.167.4.1459

J. Zhu, M. Koken, F. Quignon, M. Chelbi-alix, L. Degos et al., Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia, Proceedings of the National Academy of Sciences, vol.94, issue.8, pp.3978-3983, 1997.
DOI : 10.1073/pnas.94.8.3978

H. De-thé, L. Bras, M. Lallemand-breitenbach, and V. , Acute promyelocytic leukemia, arsenic, and PML bodies, The Journal of Cell Biology, vol.112, issue.1, pp.11-21, 2012.
DOI : 10.1016/j.ccr.2005.01.005

T. Sternsdorf, K. Jensen, and H. Will, Evidence for Covalent Modification of the Nuclear Dot???associated Proteins PML and Sp100 by PIC1/SUMO-1, The Journal of Cell Biology, vol.13, issue.7, 1997.
DOI : 10.1093/nar/24.11.2005

N. Stuurman, L. De-jong, and R. Van-driel, Nuclear frameworks: Concepts and operational definitions, Cell Biology International Reports, vol.16, issue.8, pp.837-852, 1992.
DOI : 10.1016/S0309-1651(05)80026-8

S. Bhakdi and E. Martin, Superoxide generation by human neutrophils induced by low doses of Escherichia coli hemolysin, Infect Immun, vol.59, pp.2955-2962, 1991.

M. Hamon, D. Ribet, F. Stavru, and P. Cossart, Listeriolysin O: the Swiss army knife of Listeria, Trends in Microbiology, vol.20, issue.8, pp.360-368, 2012.
DOI : 10.1016/j.tim.2012.04.006

M. Scherer, S. Klingl, M. Sevvana, V. Otto, E. Schilling et al., Crystal Structure of Cytomegalovirus IE1 Protein Reveals Targeting of TRIM Family Member PML via Coiled-Coil Interactions, PLoS Pathogens, vol.6, issue.11, p.1004512, 2014.
DOI : 10.1371/journal.ppat.1004512.s010

Y. Choi, R. Bernardi, P. Pandolfi, and E. Benveniste, The promyelocytic leukemia protein functions as a negative regulator of IFN-?? signaling, Proceedings of the National Academy of Sciences, vol.103, issue.49, pp.18715-18720, 2006.
DOI : 10.1073/pnas.0604800103

T. Ulbricht, M. Alzrigat, A. Horch, N. Reuter, A. Von-mikecz et al., PML promotes MHC class II gene expression by stabilizing the class II transactivator, The Journal of Cell Biology, vol.113, issue.1, pp.49-63, 2012.
DOI : 10.1038/35010583

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3461510

Y. Kim and J. Ahn, Positive Role of Promyelocytic Leukemia Protein in Type I Interferon Response and Its Regulation by Human Cytomegalovirus, PLOS Pathogens, vol.101, issue.7, 2015.
DOI : 10.1371/journal.ppat.1004785.s010

Y. Chen, J. Wright, X. Meng, and K. Leppard, Promyelocytic Leukemia Protein Isoform II Promotes Transcription Factor Recruitment To Activate Interferon Beta and Interferon-Responsive Gene Expression, Molecular and Cellular Biology, vol.35, issue.10, pp.1660-167201478, 2015.
DOI : 10.1128/MCB.01478-14

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4405644

E. Asmi, F. Maroui, M. Dutrieux, J. Blondel, D. Nisole et al., Implication of PMLIV in Both Intrinsic and Innate Immunity, PLoS Pathogens, vol.243, issue.2, p.1003975, 2014.
DOI : 10.1371/journal.ppat.1003975.s002

M. Scherer and T. Stamminger, Emerging Role of PML Nuclear Bodies in Innate Immune Signaling, Journal of Virology, vol.90, issue.13, pp.5850-5854, 2016.
DOI : 10.1128/JVI.01979-15

I. Rusinova, S. Forster, S. Yu, A. Kannan, M. Masse et al., INTERFEROME v2.0: an updated database of annotated interferon-regulated genes, Nucleic Acids Research, vol.41, issue.D1, pp.1040-1046, 2013.
DOI : 10.1093/nar/gks1215

R. Henry, L. Shaughnessy, M. Loessner, C. Alberti-segui, D. Higgins et al., Cytolysin-dependent delay of vacuole maturation in macrophages infected with Listeria monocytogenes, Cellular Microbiology, vol.257, issue.1, pp.107-119, 2006.
DOI : 10.1021/cr010142r

J. Malet, P. Cossart, and D. Ribet, Alteration of epithelial cell lysosomal integrity induced by bacterial cholesterol-dependent cytolysins, Cellular Microbiology, vol.17, issue.Pt A, 2016.
DOI : 10.1111/cmi.12682

Z. Wang, L. Delva, M. Gaboli, R. R. Giorgio, M. Cordon-cardo et al., Role of PML in Cell Growth and the Retinoic Acid Pathway, Science, vol.279, issue.5356, pp.1547-1551, 1998.
DOI : 10.1126/science.279.5356.1547

A. Kühbacher, P. Cossart, and J. Pizarro-cerdá, Internalization Assays for Listeria monocytogenes, Methods Mol Biol, vol.1157, pp.167-178, 2014.
DOI : 10.1007/978-1-4939-0703-8_14

R. Team, R: A language and environment for statistical computing . R Foundation for Statistical Computing, 2016.

M. Ritchie, B. Phipson, D. Wu, Y. Hu, C. Law et al., limma powers differential expression analyses for RNA-sequencing and microarray studies, Nucleic Acids Research, vol.43, issue.7, 2015.
DOI : 10.1093/nar/gkv007

URL : http://doi.org/10.1093/nar/gkv007

Y. Benjamini and Y. Hochberg, Controlling the false discovery rate: a practical and powerful approach to multiple testing, J R Stat Soc B Stat Methodol, vol.57, pp.289-300, 1995.

I. Glomski, M. Gedde, A. Tsang, J. Swanson, and D. Portnoy, hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells, The Journal of Cell Biology, vol.67, issue.6, pp.1029-1038, 2002.
DOI : 10.1073/pnas.051429498

H. Mm, 2180 NM_008302 Heat shock protein 90 alpha (cytosolic), p.956218753