G. R. Campbell and E. P. Loret, What does the structure-function relationship of the HIV-1 Tat protein teach us about developing an AIDS vaccine? Retrovirology 6, vol.50, 2009.

M. K. Johri, R. Mishra, C. Chhatbar, S. K. Unni, and S. K. Singh, Tits and bits of HIV Tat protein, Expert opinion on biological therapy, vol.11, pp.269-283, 2011.

E. Vives, P. Charneau, J. Van-rietschoten, H. Rochat, and E. Bahraoui, Effects of the Tat basic domain on human immunodeficiency virus type 1 transactivation, using chemically synthesized Tat protein and Tat peptides, Journal of virology, vol.68, pp.3343-3353, 1994.

J. E. King, E. A. Eugenin, C. M. Buckner, and J. W. Berman, HIV tat and neurotoxicity. Microbes and infection, vol.8, pp.1347-1357, 2006.

W. Li, G. Li, J. Steiner, and A. Nath, Role of Tat protein in HIV neuropathogenesis, Neurotoxicity research, vol.16, pp.205-220, 2009.

J. M. Sabatier, Evidence for neurotoxic activity of tat from human immunodeficiency virus type 1, Journal of virology, vol.65, pp.961-967, 1991.

G. R. Campbell, The glutamine-rich region of the HIV-1 Tat protein is involved in T-cell apoptosis, The Journal of biological chemistry, vol.279, pp.48197-48204, 2004.

C. J. Li, D. J. Friedman, C. Wang, V. Metelev, and A. B. Pardee, Induction of apoptosis in uninfected lymphocytes by HIV-1 Tat protein, Science, vol.268, pp.429-431, 1995.

D. Noonan and A. Albini, From the outside in: extracellular activities of HIV Tat, Adv Pharmacol, vol.48, pp.229-250, 2000.

J. C. Li, H. C. Yim, and A. S. Lau, Role of HIV-1 Tat in AIDS pathogenesis: its effects on cytokine dysregulation and contributions to the pathogenesis of opportunistic infection, AIDS, vol.24, pp.1609-1623, 2010.

G. Goldstein, HIV-1 Tat protein as a potential AIDS vaccine, Nature medicine, vol.2, pp.960-964, 1996.

M. O. Westendorp, Sensitization of T cells to CD95-mediated apoptosis by HIV-1 Tat and gp120, Nature, vol.375, pp.497-500, 1995.

H. Xiao, Selective CXCR4 antagonism by Tat: implications for in vivo expansion of coreceptor use by HIV-1, Proceedings of the National Academy of Sciences of the United States of America, vol.97, pp.11466-11471, 2000.

N. Ben-haij, K. Leghmari, R. Planes, N. Thieblemont, and E. Bahraoui, HIV-1 Tat protein binds to TLR4-MD2 and signals to induce TNF-alpha and IL-10, Retrovirology, vol.10, 2013.
URL : https://hal.archives-ouvertes.fr/inserm-00916791

K. Leghmari, Y. Bennasser, and E. Bahraoui, HIV-1 Tat protein induces IL-10 production in monocytes by classical and alternative NF-kappaB pathways, European journal of cell biology, vol.87, pp.947-962, 2008.

K. Leghmari, X. Contreras, C. Moureau, and E. Bahraoui, HIV-1 Tat protein induces TNF-alpha and IL-10 production by human macrophages: differential implication of PKC-betaII and -delta isozymes and MAP kinases ERK1/2 and p38, Cellular immunology, vol.254, pp.46-55, 2008.

K. Leghmari, Y. Bennasser, J. Tkaczuk, and E. Bahraoui, HIV-1 Tat protein induces IL-10 production by an alternative TNF-alphaindependent pathway in monocytes: role of PKC-delta and p38 MAP kinase, Cellular immunology, vol.253, pp.45-53, 2008.

S. Gupta, R. Boppana, G. C. Mishra, B. Saha, and D. Mitra, HIV-1 Tat suppresses gp120-specific T cell response in IL-10-dependent manner, J Immunol, vol.180, pp.79-88, 2008.

X. Contreras, Y. Bennasser, and E. Bahraoui, IL-10 production induced by HIV-1 Tat stimulation of human monocytes is dependent on the activation of PKC beta(II) and delta isozymes, Microbes and infection, vol.6, pp.1182-1190, 2004.

Y. Bennasser, HIV-1 Tat protein induces IL-10 production by human monocytes: implications of the PKC and calcium pathway, Journal de la Societe de biologie, vol.195, pp.319-326, 2001.

R. Masood, IL-10 inhibits HIV-1 replication and is induced by tat, Biochemical and biophysical research communications, vol.202, pp.374-383, 1994.

K. Gee, J. B. Angel, S. Mishra, M. A. Blahoianu, and A. Kumar, IL-10 regulation by HIV-Tat in primary human monocytic cells: involvement of calmodulin/calmodulin-dependent protein kinase-activated p38 MAPK and Sp-1 and CREB-1 transcription factors, J Immunol, vol.178, pp.798-807, 2007.

K. Gee, Intracellular HIV-Tat expression induces IL-10 synthesis by the CREB-1 transcription factor through Ser133 phosphorylation and its regulation by the ERK1/2 MAPK in human monocytic cells, The Journal of biological chemistry, vol.281, pp.31647-31658, 2006.

J. C. Li, D. C. Lee, B. K. Cheung, and A. S. Lau, Mechanisms for HIV Tat upregulation of IL-10 and other cytokine expression: kinase signaling and PKR-mediated immune response, FEBS letters, vol.579, pp.3055-3062, 2005.

J. K. Wong, G. R. Campbell, and S. A. Spector, Differential induction of interleukin-10 in monocytes by HIV-1 clade B and clade C Tat proteins, The Journal of biological chemistry, vol.285, pp.18319-18325, 2010.

J. C. Li and A. S. Lau, A role for mitogen-activated protein kinase and Ets-1 in the induction of interleukin-10 transcription by human immunodeficiency virus-1 Tat, Immunology, vol.121, pp.337-348, 2007.

Y. Bennasser and E. Bahraoui, HIV-1 Tat protein induces interleukin-10 in human peripheral blood monocytes: involvement of protein kinase C-betaII and -delta, FASEB journal: official publication of the Federation of American Societies for Experimental Biology, vol.16, pp.546-554, 2002.

A. Badou, Tat protein of human immunodeficiency virus type 1 induces interleukin-10 in human peripheral blood monocytes: implication of protein kinase C-dependent pathway, Journal of virology, vol.74, pp.10551-10562, 2000.

V. Blazevic, M. Heino, A. Lagerstedt, A. Ranki, and K. J. Krohn, Interleukin-10 gene expression induced by HIV-1 Tat and Rev in the cells of HIV-1 infected individuals, Journal of acquired immune deficiency syndromes and human retrovirology: official publication of the International Retrovirology Association, vol.13, pp.208-214, 1996.

W. G. Gutheil, Human immunodeficiency virus 1 Tat binds to dipeptidyl aminopeptidase IV (CD26): a possible mechanism for Tat's immunosuppressive activity, Proceedings of the National Academy of Sciences of the United States of America, vol.91, pp.6594-6598, 1994.

M. R. Zocchi, A. Rubartelli, P. Morgavi, and A. Poggi, HIV-1 Tat inhibits human natural killer cell function by blocking L-type calcium channels, J Immunol, vol.161, pp.2938-2943, 1998.

M. R. Zocchi, A. Poggi, and A. Rubartelli, The RGD-containing domain of exogenous HIV-1 Tat inhibits the engulfment of apoptotic bodies by dendritic cells, AIDS, vol.11, pp.1227-1235, 1997.

A. Albini, The angiogenesis induced by HIV-1 tat protein is mediated by the Flk-1/KDR receptor on vascular endothelial cells, Nature medicine, vol.2, pp.1371-1375, 1996.

E. Hui, T cell costimulatory receptor CD28 is a primary target for PD-1-mediated inhibition, Science, vol.355, pp.1428-1433, 2017.

R. Planes, HIV-1 Tat protein induces PD-L1 (B7-H1) expression on dendritic cells through tumor necrosis factor alpha-and toll-like receptor 4-mediated mechanisms, Journal of virology, vol.88, pp.6672-6689, 2014.

R. Planes and E. Bahraoui, HIV-1 Tat protein induces the production of IDO in human monocyte derived-dendritic cells through a direct mechanism: effect on T cells proliferation, PloS one, vol.8, 2013.
URL : https://hal.archives-ouvertes.fr/inserm-00873100

T. Samikkannu, Differential regulation of indoleamine-2,3-dioxygenase (IDO) by HIV type 1 clade B and C Tat protein, AIDS research and human retroviruses, vol.25, pp.329-335, 2009.

M. A. Lawson, K. W. Kelley, and R. Dantzer, Intracerebroventricular administration of HIV-1 Tat induces brain cytokine and indoleamine 2,3-dioxygenase expression: a possible mechanism for AIDS comorbid depression, Brain, behavior, and immunity, vol.25, pp.1569-1575, 2011.

A. L. Mellor and D. H. Munn, IDO expression by dendritic cells: tolerance and tryptophan catabolism, Nature reviews. Immunology, vol.4, pp.762-774, 2004.

W. Chen, IDO: more than an enzyme, Nature immunology, vol.12, pp.809-811, 2011.

Y. Koide, K. Ryu, and T. O. Yoshida, The signal transduction mechanism responsible for interferon-gamma-inducible indoleamine 2,3-dioxygenase (IDO) gene expression in T98G cells

Z. Nihon-saikingaku, Japanese journal of bacteriology, vol.47, pp.689-694, 1992.

M. P. Heyes, Relationship between interferon-gamma, indoleamine-2,3-dioxygenase and tryptophan, FASEB journal: official publication of the Federation of American Societies for Experimental Biology, vol.5, pp.3003-3004, 1991.

M. W. Taylor and G. S. Feng, Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism, FASEB journal: official publication of the Federation of American Societies for Experimental Biology, vol.5, pp.2516-2522, 1991.

N. Ben-haij, HIV-1 Tat Protein Induces Production of Proinflammatory Cytokines by Human Dendritic Cells and Monocytes/ Macrophages through Engagement of TLR4-MD2-CD14 Complex and Activation of NF-kappaB Pathway, PloS one, vol.10, 2015.

S. R. Coats, T. T. Pham, B. W. Bainbridge, R. A. Reife, and R. P. Darveau, MD-2 mediates the ability of tetra-acylated and pentaacylated lipopolysaccharides to antagonize Escherichia coli lipopolysaccharide at the TLR4 signaling complex, J Immunol, vol.175, pp.4490-4498, 2005.

D. G. Smith, Quinolinic acid is produced by macrophages stimulated by platelet activating factor, Nef and Tat, Journal of neurovirology, vol.7, pp.56-60, 2001.

A. Boasso, HIV inhibits CD4+ T-cell proliferation by inducing indoleamine 2,3-dioxygenase in plasmacytoid dendritic cells, Blood, vol.109, pp.3351-3359, 2007.

J. A. Martinson, Chloroquine modulates HIV-1-induced plasmacytoid dendritic cell alpha interferon: implication for T-cell activation, Antimicrobial agents and chemotherapy, vol.54, pp.871-881, 2010.

D. Favre, Tryptophan catabolism by indoleamine 2,3-dioxygenase 1 alters the balance of TH17 to regulatory T cells in HIV disease, Science translational medicine, vol.2, pp.32-36, 2010.

M. P. Heyes, Elevated cerebrospinal fluid quinolinic acid levels are associated with region-specific cerebral volume loss in HIV infection, Brain: a journal of neurology, vol.124, pp.1033-1042, 2001.

J. C. Mbongue, The Role of Indoleamine 2, 3-Dioxygenase in Immune Suppression and Autoimmunity, vol.3, pp.703-729, 2015.

Y. Kudo, The role of placental indoleamine 2,3-dioxygenase in human pregnancy, Obstetrics & gynecology science, vol.56, pp.209-216, 2013.

A. Honig, Indoleamine 2,3-dioxygenase (IDO) expression in invasive extravillous trophoblast supports role of the enzyme for materno-fetal tolerance, Journal of reproductive immunology, vol.61, pp.79-86, 2004.

J. Y. Zhang, PD-1 up-regulation is correlated with HIV-specific memory CD8+ T-cell exhaustion in typical progressors but not in long-term nonprogressors, Blood, vol.109, pp.4671-4678, 2007.

X. Wang, B7-H1 up-regulation impairs myeloid DC and correlates with disease progression in chronic HIV-1 infection, European journal of immunology, vol.38, pp.3226-3236, 2008.

M. A. Brockman, IL-10 is up-regulated in multiple cell types during viremic HIV infection and reversibly inhibits virus-specific T cells, Blood, vol.114, pp.346-356, 2009.

R. Planes, HIV-1 Tat Protein Activates both the MyD88 and TRIF Pathways To Induce Tumor Necrosis Factor Alpha and Interleukin-10 in Human Monocytes, Journal of virology, vol.90, pp.5886-5898, 2016.

H. Wu, J. Gong, and Y. Liu, Indoleamine 2, 3-dioxygenase regulation of immune response (Review), Molecular medicine reports, vol.17, pp.4867-4873, 2018.

C. Orabona, Enhanced tryptophan catabolism in the absence of the molecular adapter DAP12, European journal of immunology, vol.35, pp.3111-3118, 2005.
URL : https://hal.archives-ouvertes.fr/hal-00079613

C. Orabona, SOCS3 drives proteasomal degradation of indoleamine 2,3-dioxygenase (IDO) and antagonizes IDO-dependent tolerogenesis, Proceedings of the National Academy of Sciences of the United States of America 105, pp.20828-20833, 2008.