Abstract
The cofactors nicotinamide adenine dinucleotide (NAD+) and its phosphate form, NADP+, are crucial molecules present in all living cells. The delicate balance between the oxidized and reduced forms of these molecules is tightly regulated by intracellular metabolism assuring the maintenance of homeostatic conditions, which are essential for cell survival and proliferation. A recent cluster of data has highlighted the importance of the intracellular NAD+/NADH and NADP+/NADPH ratios during host–pathogen interactions, as fluctuations in the levels of these cofactors and in precursors’ bioavailability may condition host response and, therefore, pathogen persistence or elimination. Furthermore, an increasing interest has been given towards how pathogens are capable of hijacking host cell proteins in their own advantage and, consequently, alter cellular redox states and immune function. Here, we review the basic principles behind biosynthesis and subcellular compartmentalization of NAD+ and NADP+, as well as the importance of these cofactors during infection, with a special emphasis on pathogen-driven modulation of host NAD+/NADP+ levels and contribution to the associated immune response.
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References
Bastiat-Sempe B, Love JF, Lomayesva N, Wessels MR (2014) Streptolysin O and NAD-glycohydrolase prevent phagolysosome acidification and promote group A Streptococcus survival in macrophages. MBio 5:e01690-14
Bellac CL, Coimbra RS, Christen S, Leib SL (2006) Pneumococcal meningitis causes accumulation of neurotoxic kynurenine metabolites in brain regions prone to injury. Neurobiol Dis 24:395–402
Bellac CL, Coimbra RS, Christen S, Leib SL (2010) Inhibition of the Kynurenine-NAD + pathway leads to energy failure and exacerbates apoptosis in pneumococcal meningitis. J Neuropathol Exp Neurol 69:1096–1104
Bianchi M, Hakkim A, Brinkmann V, Siler U, Seger RA, Zychlinsky A, Reichenbach J (2009) Restoration of NET formation by gene therapy in CGD controls aspergillosis. Blood 114:2619–2622
Bianchi M, Niemiec MJ, Siler U, Urban CF, Reichenbach J (2011) Restoration of anti-Aspergillus defense by neutrophil extracellular traps in human chronic granulomatous disease after gene therapy is calprotectin-dependent. J Allergy Clin Immunol 127:1243–1252
Boasso A, Herbeuval JP, Hardy AW, Anderson SA, Dolan MJ, Fuchs D, Shearer GM (2007) HIV inhibits CD4+ T-cell proliferation by inducing indoleamine 2,3-dioxygenase in plasmacytoid dendritic cells. Blood 109:3351–3359
Boasso A, Hardy AW, Anderson SA, Dolan MJ, Shearer GM (2008) HIV-induced type I interferon and tryptophan catabolism drive T cell dysfunction despite phenotypic activation. PLoS One 3:e2961
Brown SA, Palmer KL, Whiteley M (2008) Revisiting the host as a growth medium. Nat Rev Microbiol 6:657–666
Cardoso F, Castro F, Moreira-Teixeira L, Sousa J, Torrado E, Silvestre R, Castro AG, Saraiva M, Pais TF (2015) Myeloid sirtuin 2 expression does not impact long-term Mycobacterium tuberculosis control. PLoS One 10:e0131904
Cheng SC, Scicluna BP, Arts RJW, Gresnigt MS, Lachmandas E, Giamarellos-Bourboulis EJ, Kox M, Manjeri GR, Wagenaars JAL, Cremer OL et al (2016) Broad defects in the energy metabolism of leukocytes underlie immunoparalysis in sepsis. Nat Immunol 17:406–413
Cheng CY, Gutierrez NM, Marzuki MB, Lu X, Foreman TW, Paleja B, Lee B, Balachander A, Chen J, Tsenova L et al (2017) Host sirtuin 1 regulates mycobacterial immunopathogenesis and represents a therapeutic target against tuberculosis. Sci Immunol 2:eaaj1789
Cheong W-C, Park J-H, Kang H-R, Song MJ (2015) Down-regulation of poly (ADP-ribose) polymerase-1 by a viral processivity factor facilitates gammaherpesvirus lytic replication. J Virol 89:9676–9682
Conti F, Lugo-Reyes SO, Blancas Galicia L, He J, Aksu G, Borges de Oliveira E, Deswarte C, Hubeau M, Karaca N, de Suremain M et al (2016) Mycobacterial disease in patients with chronic granulomatous disease: a retrospective analysis of 71 cases. J Allergy Clin Immunol 138:241–248.e3
de Toledo FG, Cheng J, Liang M, Chini EN, Dousa TP (2000) ADP-Ribosyl cyclase in rat vascular smooth muscle cells: properties and regulation. Circ Res 86:1153–1159
Deffert C, Cachat J, Krause K-H (2014) Phagocyte NADPH oxidase, chronic granulomatous disease and mycobacterial infections. Cell Microbiol 16:1168–1178
Di Stefano M, Conforti L (2013) Diversification of NAD biological role: the importance of location. FEBS J 280:4711–4728
Dölle C, Niere M, Lohndal E, Ziegler M (2010) Visualization of subcellular NAD pools and intra-organellar protein localization by poly-ADP-ribose formation. Cell Mol Life Sci 67:433–443
Dousa TP, Chini EN, Beers KW (1996) Adenine nucleotide diphosphates: emerging second messengers acting via intracellular Ca2+ release. Am J Physiol 271:C1007–C1024
El-Zaatari M, Chang Y-M, Zhang M, Franz M, Shreiner A, McDermott AJ, van der Sluijs KF, Lutter R, Grasberger H, Kamada N et al (2014) Tryptophan catabolism restricts IFN-γ–expressing neutrophils and Clostridium difficile immunopathology. J Immunol 193:807–816
Eskandarian HA, Impens F, Nahori M-A, Soubigou G, Coppee J-Y, Cossart P, Hamon MA (2013) A role for SIRT2-dependent histone H3K18 deacetylation in bacterial infection. Science 341:1238858
Estrada-Figueroa LA, Ramírez-Jiménez Y, Osorio-Trujillo C, Shibayama M, Navarro-García F, García-Tovar C, Talamás-Rohana P (2011) Absence of CD38 delays arrival of neutrophils to the liver and innate immune response development during hepatic amoebiasis by Entamoeba histolytica. Parasite Immunol 33:661–668
Fallarino F, Grohmann U, You S, McGrath BC, Cavener DR, Vacca C, Orabona C, Bianchi R, Belladonna ML, Volpi C et al (2006) The combined effects of tryptophan starvation and tryptophan catabolites down-regulate T Cell receptor-chain and induce a regulatory phenotype in naive T cells. J Immunol 176:6752–6761
Fan J, Ye J, Kamphorst JJ, Shlomi T, Thompson CB, Rabinowitz JD (2014) Quantitative flux analysis reveals folate-dependent NADPH production. Nature 510:298–302
Gameiro PA, Laviolette LA, Kelleher JK, Iliopoulos O, Stephanopoulos G (2013) Cofactor balance by nicotinamide nucleotide transhydrogenase (NNT) coordinates reductive carboxylation and glucose catabolism in the tricarboxylic acid (TCA) cycle. J Biol Chem 288:12967–12977
Ganesan R, Hos NJ, Gutierrez S, Fischer J, Stepek JM, Daglidu E, Krönke M, Robinson N (2017) Salmonella Typhimurium disrupts Sirt1/AMPK checkpoint control of mTOR to impair autophagy. PLoS Pathog 13:e1006227
Grez M, Reichenbach J, Schwäble J, Seger R, Dinauer MC, Thrasher AJ (2011) Gene therapy of chronic granulomatous disease: the engraftment dilemma. Mol Ther 19:28–35
Gurtner GJ, Newberry RD, Schloemann SR, McDonald KG, Stenson WF (2003) Inhibition of indoleamine 2,3-dioxygenase augments trinitrobenzene sulfonic acid colitis in mice. Gastroenterology 125:1762–1773
Gutierrez DA, Valdes L, Serguera C, Llano M (2016) Poly(ADP-ribose) polymerase-1 silences retroviruses independently of viral DNA integration or heterochromatin formation. J Gen Virol 97:1686–1692
Ha E-M (2005) A direct role for dual oxidase in Drosophila gut immunity. Science 310:847–850
Ha HC, Juluri K, Zhou Y, Leung S, Hermankova M, Snyder SH (2001) Poly(ADP-ribose) polymerase-1 is required for efficient HIV-1 integration. Proc Natl Acad Sci U S A 98:3364–3368
He M, Gao SJ (2014) A novel role of SIRT1 in gammaherpesvirus latency and replication. Cell Cycle 13:3328–3330
Hogan D, Wheeler RT (2014) The complex roles of NADPH oxidases in fungal infection. Cell Microbiol 16:1156–1167
Houtkooper RH, Pirinen E, Auwerx J (2012) Sirtuins as regulators of metabolism and healthspan. Nat Rev Mol Cell Biol 13:225–238
Kameoka M, Nukuzuma S, Itaya A, Tanaka Y, Ota K, Inada Y, Ikuta K, Yoshihara K (2005) Poly(ADP-ribose)polymerase-1 is required for integration of the human immunodeficiency virus type 1 genome near centromeric alphoid DNA in human and murine cells. Biochem Biophys Res Commun 334:412–417
Kim S-H, Lee W-J (2014) Role of DUOX in gut inflammation: lessons from Drosophila model of gut-microbiota interactions. Front Cell Infect Microbiol 3:116
Kim UH, Kim MK, Kim JS, Han MK, Park BH, Kim HR (1993) Purification and characterization of NAD glycohydrolase from rabbit erythrocytes. Arch Biochem Biophys 305:147–152
Koedel U, Winkler F, Angele B, Fontana A, Pfister HW (2002) Meningitis-associated central nervous system complications are mediated by the activation of poly(ADP-ribose) polymerase. J Cereb Blood Flow Metab 22:39–49
Lau C, Dölle C, Gossmann TI, Agledal L, Niere M, Ziegler M (2010) Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases. J Biol Chem 285:18868–18876
Lee WP, Hou MC, Lan KH, Li CP, Chao Y, Lin HC, Lee SD (2016) Helicobacter pylori-induced chronic inflammation causes telomere shortening of gastric mucosa by promoting PARP-1-mediated non-homologous end joining of DNA. Arch Biochem Biophys 606:90–98
Lewis CA, Parker SJ, Fiske BP, McCloskey D, Gui DY, Green CR, Vokes NI, Feist AM, Vander Heiden MG, Metallo CM (2014) Tracing compartmentalized NADPH metabolism in the cytosol and mitochondria of mammalian cells. Mol Cell 55:253–263
Li W, Katz BP, Spinola SM (2011) Haemophilus ducreyi lipooligosaccharides induce expression of the immunosuppressive enzyme indoleamine 2,3-dioxygenase via type I interferons and tumor necrosis factor alpha in human dendritic cells. Infect Immun 79:3338–3347
Li Q, He M, Zhou F, Ye F, Gao S-J (2014) Activation of Kaposi’s sarcoma-associated herpesvirus (KSHV) by inhibitors of class III histone deacetylases: identification of sirtuin 1 as a regulator of the KSHV life cycle. J Virol 88:6355–6367
Lischke T, Heesch K, Schumacher V, Schneider M, Haag F, Koch-Nolte F, Mittrücker HW (2013) CD38 controls the innate immune response against listeria monocytogenes. Infect Immun 81:4091–4099
Liu TF, Vachharajani VT, Yoza BK, McCall CE (2012) NAD+-dependent sirtuin 1 and 6 proteins coordinate a switch from glucose to fatty acid oxidation during the acute inflammatory response. J Biol Chem 287:25758–25769
Liu W, Lin Y, Xiao H, Xing S, Chen H, Chi P, Zhang G (2014) Epstein-Barr virus infection induces indoleamine 2,3-dioxygenase expression in human monocyte-derived macrophages through p38/mitogen-activated protein kinase and NF-κB pathways: impairment in T cell functions. J Virol 88:6660–6671
Liu TF, Vachharajani V, Millet P, Bharadwaj MS, Molina AJ, McCall CE (2015) Sequential actions of SIRT1-RELB-SIRT3 coordinate nuclear-mitochondrial communication during immunometabolic adaptation to acute inflammation and sepsis. J Biol Chem 290:396–408
Liu L, Shah S, Fan J, Park JO, Wellen KE, Rabinowitz JD (2016) Malic enzyme tracers reveal hypoxia-induced switch in adipocyte NADPH pathway usage. Nat Chem Biol 12:345–352
Lupey-Green LN, Moquin SA, Martin KA, McDevitt SM, Hulse M, Caruso LB, Pomerantz RT, Miranda JL, Tempera I (2017) PARP1 restricts Epstein Barr Virus lytic reactivation by binding the BZLF1 promoter. Virology 507:220–230
Magni G (2008) Enzymology of mammalian NAD metabolism in health and disease. Front Biosci 3:6135
Martin KA, Lupey LN, Tempera I (2016) Epstein-Barr Virus oncoprotein LMP1 mediates epigenetic changes in host gene expression through PARP1. J Virol 90:8520–8530
Matalonga J, Glaria E, Bresque M, Escande C, Carbó JM, Kiefer K, Vicente R, León TE, Beceiro S, Pascual-García M et al (2017) The nuclear receptor LXR limits bacterial infection of host macrophages through a mechanism that impacts cellular NAD metabolism. Cell Rep 18:1241–1255
Medana IM, Mai NTH, Day NPJ, Hien TT, Bethell D, Phu NH, Farrar J, White NJ, Turner GDH (2001) Cellular stress and injury responses in the brains of adult Vietnamese patients with fatal Plasmodium falciparum malaria. Neuropathol Appl Neurobiol 27:421–433
Mesquita I, Varela P, Belinha A, Gaifem J, Laforge M, Vergnes B, Estaquier J, Silvestre R (2016) Exploring NAD+ metabolism in host-pathogen interactions. Cell Mol Life Sci 73:1225–1236
Michan S, Sinclair D (2007) Sirtuins in mammals: insights into their biological function. Biochem J 404:1–13
Michos A, Gryllos I, Håkansson A, Srivastava A, Kokkotou E, Wessels MR (2006) Enhancement of streptolysin O activity and intrinsic cytotoxic effects of the group A streptococcal toxin, NAD-glycohydrolase. J Biol Chem 281:8216–8223
Mittal M, Siddiqui MR, Tran K, Reddy SP, Malik AB (2014) Reactive oxygen species in inflammation and tissue injury. Antioxid Redox Signal 20:1126–1167
Moreira D, Rodrigues V, Abengozar M, Rivas L, Rial E, Laforge M, Li X, Foretz M, Viollet B, Estaquier J et al (2015) Leishmania infantum modulates host macrophage mitochondrial metabolism by hijacking the SIRT1-AMPK axis. PLoS Pathog 11:1–24
Moreschi I, Bruzzone S, Nicholas RA, Fruscione F, Sturla L, Benvenuto F, Usai C, Meis S, Kassack MU, Zocchi E et al (2006) Extracellular NAD+ is an agonist of the human P2Y 11 purinergic receptor in human granulocytes. J Biol Chem 281:31419–31429
Mori V, Amici A, Mazzola F, Di Stefano M, Conforti L, Magni G, Ruggieri S, Raffaelli N, Orsomando G (2014) Metabolic profiling of alternative NAD biosynthetic routes in mouse tissues. PLoS One 9:e113939
Müller S (2004) Redox and antioxidant systems of the malaria parasite Plasmodium falciparum. Mol Microbiol 53:1291–1305
Munn DH, Mellor AL (2013) Indoleamine 2,3 dioxygenase and metabolic control of immune responses. Trends Immunol 34:137–143
Murray MF, Srinivasan A (1995) Nicotinamide inhibits HIV-1 in both acute and chronic in vitro infection. Biochem Biophys Res Commun 210:954–959
Murray MF, Nghiem M, Srinivasan A (1995) HIV infection decreases intracellular nicotinamide adenine dinucleotide [NAD]. Biochem Biophys Res Commun 212:126–131
Navarro J, Gozalbo-López B, Méndez AC, Dantzer F, Schreiber V, Martínez C, Arana DM, Farrés J, Revilla-Nuin B, Bueno MF et al (2017) PARP-1/PARP-2 double deficiency in mouse T cells results in faulty immune responses and T lymphomas. Sci Rep 7:41962
O’Seaghdha M, Wessels MR (2013) Streptolysin O and its co-toxin NAD-glycohydrolase protect group A Streptococcus from xenophagic killing. PLoS Pathog 9:e1003394
Olszewski KL, Morrisey JM, Wilinski D, Burns JM, Vaidya AB, Rabinowitz JD, Llinás M (2009) Host-parasite interactions revealed by Plasmodium falciparum metabolomics. Cell Host Microbe 5:191–199
Paiva CN, Bozza MT (2014) Are reactive oxygen species always detrimental to pathogens? Antioxid Redox Signal 20:1000–1037
Palmer CS, Cherry CL, Sada-Ovalle I, Singh A, Crowe SM (2016) Glucose metabolism in T cells and monocytes: new perspectives in HIV pathogenesis. EBioMedicine 6:31–41
Panday A, Sahoo MK, Osorio D, Batra S (2015) NADPH oxidases: an overview from structure to innate immunity-associated pathologies. Cell Mol Immunol 12:5–23
Partida-Sánchez S, Cockayne DA, Monard S, Jacobson EL, Oppenheimer N, Garvy B, Kusser K, Goodrich S, Howard M, Harmsen A et al (2001) Cyclic ADP-ribose production by CD38 regulates intracellular calcium release, extracellular calcium influx and chemotaxis in neutrophils and is required for bacterial clearance in vivo. Nat Med 7:1209–1216
Partidá-Sánchez S, Rivero-Nava L, Shi G, Lund FE (2007) CD38: an ecto-enzyme at the crossroads of innate and adaptive immune responses. Adv Exp Med Biol 590:171–183
Peek CB, Affinati AH, Ramsey KM, Kuo H-Y, Yu W, Sena LA, Ilkayeva O, Marcheva B, Kobayashi Y, Omura C et al (2013) Circadian clock NAD+ cycle drives mitochondrial oxidative metabolism in mice. Science 342:1243417–1243417
Pircalabioru G, Aviello G, Kubica M, Zhdanov A, Paclet MH, Brennan L, Hertzberger R, Papkovsky D, Bourke B, Knaus UG (2016) Defensive mutualism rescues NADPH oxidase inactivation in gut infection. Cell Host Microbe 19:651–663
Pittelli M, Formentini L, Faraco G, Lapucci A, Rapizzi E, Cialdai F, Romano G, Moneti G, Moroni F, Chiarugi A (2010) Inhibition of nicotinamide phosphoribosyltransferase: cellular bioenergetics reveals a mitochondrial insensitive NAD pool. J Biol Chem 285:34106–34114
Pollak N, Dölle C, Ziegler M (2007) The power to reduce: pyridine nucleotides – small molecules with a multitude of functions. Biochem J 402:205–218
Potula R, Poluektova L, Knipe B, Chrastil J, Heilman D, Dou H, Takikawa O, Munn DH, Gendelman HE, Persidsky Y (2005) Inhibition of indoleamine 2,3-dioxygenase (IDO) enhances elimination of virus-infected macrophages in an animal model of HIV-1 encephalitis. Blood 106:2382–2390
Prendergast GC, Smith C, Thomas S, Mandik-Nayak L, Laury-Kleintop L, Metz R, Muller AJ (2014) Indoleamine 2,3-dioxygenase pathways of pathogenic inflammation and immune escape in cancer. Cancer Immunol Immunother 63:721–735
Rada B, Leto T (2008) Oxidative innate immune defenses by Nox/Duox family NADPH oxidases. Contrib Microbiol 15:164–187
Ren J-H, Tao Y, Zhang Z-Z, Chen W-X, Cai X-F, Chen K, Ko BCB, Song C-L, Ran L-K, Li W-Y et al (2014) Sirtuin 1 regulates hepatitis B virus transcription and replication by targeting transcription factor AP-1. J Virol 88:2442–2451
Revollo JR, Körner A, Mills KF, Satoh A, Wang T, Garten A, Dasgupta B, Sasaki Y, Wolberger C, Townsend RR et al (2007) Nampt/PBEF/Visfatin regulates insulin secretion in beta cells as a systemic NAD biosynthetic enzyme. Cell Metab 6:363–375
Rom S, Reichenbach NL, Dykstra H, Persidsky Y (2015) The dual action of poly(ADP-ribose) polymerase-1 (PARP-1) inhibition in HIV-1 infection: HIV-1 ltr inhibition and diminution in Rho GTPase activity. Front Microbiol 6:878
Schmidt SV, Schultze JL (2014) New insights into IDO biology in bacterial and viral infections. Front Immunol 5:384
Schreiber V, Dantzer F, Amé JC, De Murcia G (2006) Poly(ADP-ribose): novel functions for an old molecule. Nat Rev Mol Cell Biol 7:517–528
Segal BH, Romani LR (2009) Invasive aspergillosis in chronic granulomatous disease. Med Mycol 47(Suppl 1):S282–S290
Seman M, Adriouch S, Haag F, Koch-Nolte F (2004) Ecto-ADP-ribosyltransferases (ARTs): emerging actors in cell communication and signaling. Curr Med Chem 11:857–872
Sharma O, O’Seaghdha M, Velarde JJ, Wessels MR (2016) NAD+-glycohydrolase promotes intracellular survival of group A Streptococcus. PLoS Pathog 12:e1005468
Siva AC, Bushman F (2002) Poly(ADP-ribose) polymerase 1 is not strictly required for infection of murine cells by retroviruses. J Virol 76:11904–11910
Sodhi RK, Singh N, Jaggi AS (2010) Poly(ADP-ribose) polymerase-1 (PARP-1) and its therapeutic implications. Vascul Pharmacol 53:77–87
Tatsuno I, Isaka M, Minami M, Hasegawa T (2010) NADase as a target molecule of in vivo suppression of the toxicity in the invasive M-1 group A Streptococcal isolates. BMC Microbiol 10:144
Thakur BK, Chandra A, Dittrich T, Welte K, Chandra P (2012) Inhibition of SIRT1 by HIV-1 viral protein Tat results in activation of p53 pathway. Biochem Biophys Res Commun 424:245–250
Tibbetts AS, Appling DR (2010) Compartmentalization of mammalian folate-mediated one-carbon metabolism. Annu Rev Nutr 30:57–81
Uyoga S, Ndila CM, Macharia AW, Nyutu G, Shah S, Peshu N, Clarke GM, Kwiatkowski DP, Rockett KA, Williams TN (2015) Glucose-6-phosphate dehydrogenase deficiency and the risk of malaria and other diseases in children in Kenya: a case-control and a cohort study. Lancet Haematol 2:e437–e444
Van Assche T, Deschacht M, Da Luz RAI, Maes L, Cos P (2011) Leishmania-macrophage interactions: insights into the redox biology. Free Radic Biol Med 51:337–351
Van den Bergh R, Florence E, Vlieghe E, Boonefaes T, Grooten J, Houthuys E, Tran H, Gali Y, De Baetselier P, Vanham G et al (2010) Transcriptome analysis of monocyte-HIV interactions. Retrovirology 7:53
VanLinden MR, Dölle C, Pettersen IK, Kulikova VA, Niere M, Agrimi G, Dyrstad SE, Palmieri F, Nikiforov AA, Tronstad KJ, Ziegler M (2015) Subcellular distribution of NAD+ between cytosol and mitochondria determines the metabolic profile of human cells. J Biol Chem 290(46):27644–27659. https://doi.org/10.1074/jbc.M115.654129
Viegas MS, do Carmo A, Silva T, Seco F, Serra V, Lacerda M, Martins TC (2007) CD38 plays a role in effective containment of mycobacteria within granulomata and polarization of Th1 immune responses against Mycobacterium avium. Microbes Infect 9:847–854
Vujkovic-Cvijin I, Swainson LA, Chu SN, Ortiz AM, Santee CA, Petriello A, Dunham RM, Fadrosh DW, Lin DL, Faruqi AA et al (2015) Gut-resident Lactobacillus abundance associates with IDO1 inhibition and Th17 dynamics in SIV-infected macaques. Cell Rep 13:1589–1597
Wan X, Wen JJ, Koo SJ, Liang LY, Garg NJ (2016) SIRT1-PGC1α-NFκB pathway of oxidative and inflammatory stress during Trypanosoma cruzi infection: benefits of SIRT1-targeted therapy in improving heart function in Chagas disease. PLoS Pathog. 12:e1005954
Wang G, Huang X, Li Y, Guo K, Ning P, Zhang Y (2013) PARP-1 inhibitor, DPQ, attenuates LPS-induced acute lung injury through inhibiting NF-κB-mediated inflammatory response. PLoS One 8:e79757
Williamson D, Lund P, Krebs H (1967) The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J 103:514–527
Wise DR, Ward PS, Shay JES, Cross JR, Gruber JJ, Sachdeva UM, Platt JM, DeMatteo RG, Simon MC, Thompson CB (2011) Hypoxia promotes isocitrate dehydrogenase-dependent carboxylation of -ketoglutarate to citrate to support cell growth and viability. Proc Natl Acad Sci 108:19611–19616
Wu X, Deng G, Li M, Li Y, Ma C, Wang Y, Liu X (2015) Wnt/β-Catenin signaling reduces Bacillus Calmette-Guerin-induced macrophage necrosis through a ROS-mediated PARP/AIF-dependent pathway. BMC Immunol 16:16
Xie H, Lei N, Gong AY, Chen XM, Hu G (2014) Cryptosporidium parvum induces SIRT1 expression in host epithelial cells through downregulating let-7i. Hum Immunol 75:760–765
Yang H, Yang T, Baur JA, Perez E, Matsui T, Carmona JJ, Lamming DWW, Souza-Pinto NC, Bohr VA, Rosenzweig A et al (2007) Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival. Cell 130:1095–1107
Yeung AWS, Wu W, Freewan M, Stocker R, King NJC, Thomas SR (2012) Flavivirus infection induces indoleamine 2,3-dioxygenase in human monocyte-derived macrophages via tumor necrosis factor and NF-κB. J Leukoc Biol 91:657–666
Yu SW, Wang H, Poitras MF, Coombs C, Bowers WJ, Federoff HJ, Poirier GG, Dawson TM, Dawson VL (2002) Mediation of poly(ADP-ribose) polymerase-1 – dependent cell death by apoptosis-inducing factor. Science 297:259–263
Zerez CR, Roth EF, Schulman S, Tanaka KR (1990) Increased nicotinamide adenine dinucleotide content and synthesis in Plasmodium falciparum-infected human erythrocytes. Blood 75:1705–1710
Zhang HS, Zhou Y, Wu MR, Zhou HS, Xu F (2009) Resveratrol inhibited Tat-induced HIV-1 LTR transactivation via NAD+-dependent SIRT1 activity. Life Sci 85:484–489
Zhang H-S, Sang W-W, Wang Y-O, Liu W (2010) Nicotinamide phosphoribosyltransferase/sirtuin 1 pathway is involved in human immunodeficiency virus type 1 Tat-mediated long terminal repeat transactivation. J Cell Biochem 110:1464–1470
Zhang HS, Chen XY, Wu TC, Zhang FJ (2014) Tanshinone II A inhibits tat-induced HIV-1 transactivation through redox-regulated AMPK/Nampt pathway. J Cell Physiol 229:1193–1201
Funding Statement
This work was supported by the Northern Portugal Regional Operational Programme (NORTE 2020), under the Portugal 2020 Partnership Agreement, through the European Regional Development Fund (FEDER) (NORTE-01-0145-FEDER-000013) and the Fundação para a Ciência e Tecnologia (FCT) (contracts SFRH/BD/120127/2016 to IM and IF/00021/2014 to RS), and Infect-Era (project INLEISH).
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Mesquita, I., Vergnes, B., Silvestre, R. (2018). Alterations on Cellular Redox States upon Infection and Implications for Host Cell Homeostasis. In: Silvestre, R., Torrado, E. (eds) Metabolic Interaction in Infection. Experientia Supplementum, vol 109. Springer, Cham. https://doi.org/10.1007/978-3-319-74932-7_4
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