Cited by 346Mitochondrial Function and PathologyAutophagy in Disease and TherapyImmune Response and Inflammation

Mitochondria as a Cellular Hub in Infection and Inflammation

Open access
Andrieux, Pauline, Chevillard, Christophe, Cunha-Neto, Edecio, Nunes, João Paulo Silva·2021·International Journal of Molecular Sciences

Abstract

Mitochondria are the energy center of the cell. They are found in the cell cytoplasm as dynamic networks where they adapt energy production based on the cell’s needs. They are also at the center of the proinflammatory response and have essential roles in the response against pathogenic infections. Mitochondria are a major site for production of Reactive Oxygen Species (ROS; or free radicals), which are essential to fight infection. However, excessive and uncontrolled production can become deleterious to the cell, leading to mitochondrial and tissue damage. Pathogens exploit the role of mitochondria during infection by affecting the oxidative phosphorylation mechanism (OXPHOS), mitochondrial network and disrupting the communication between the nucleus and the mitochondria. The role of mitochondria in these biological processes makes these organelle good targets for the development of therapeutic strategies. In this review, we presented a summary of the endosymbiotic origin of mitochondria and their involvement in the pathogen response, as well as the potential promising mitochondrial targets for the fight against infectious diseases and chronic inflammatory diseases.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/ijms222111338

Cites

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Pathogenic microorganisms such as viruses are usually detected by specific cell protein complexes through recognition of pathogen-associated molecular patterns (PAMPs), including LPS.

    “pathogenic microorganisms such as viruses are usually detected by specific cell protein complexes through the recognition of pathogen-associated molecular patterns (PAMPs), including LPS [51].”

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The citation lists haven’t been fetched yet

References 266 · Cited by 346

Research works printed but not linked: 244

  1. [1]Mileykovskaya E. Dowhan W. Cardiolipin membrane domains in prokaryotes and eukaryotes Biochim. Biophys. Acta (BBA) Biomembr. 2009 1788 2084 2091 10.1016/j.bbamem.2009.04.003 19371718 PMC2757463 · DOI
  2. [2]Nass S. Nass M.M. Intramitochondrial Fibers with DNA Characteristics. Ii. Enzymatic and Other Hydrolytic Treatments J. Cell Biol. 1963 19 613 629 10.1083/jcb.19.3.613 14086139 PMC2106332 · DOI
  3. [3]Sagan L. On the origin of mitosing cells J. Theor. Biol. 1967 14 225 274 10.1016/0022-5193(67)90079-3 11541392 · DOI · Paper page
  4. [5]Gould S.B. Garg S.G. Martin W.F. Bacterial Vesicle Secretion and the Evolutionary Origin of the Eukaryotic Endomembrane System Trends Microbiol. 2016 24 525 534 10.1016/j.tim.2016.03.005 27040918 · DOI
  5. [6]Anderson S. Bankier A.T. Barrell B.G. De Bruijn M.H.L. Coulson A.R. Drouin J. Eperon I. Nierlich D.P. Roe B.A. Sanger F. Sequence and organization of the human mitochondrial genome Nature 1981 290 457 465 10.1038/290457a0 7219534 · DOI
  6. [7]Gray M. Sankoff D. Cedergren R.J. On the evolutionary descent of organisms and organelles: A global phylogeny based on a highly conserved structural core in small subunit ribosomal RNA Nucleic Acids Res. 1984 12 5837 5852 10.1093/nar/12.14.5837 6462918 PMC320035 · DOI
  7. [8]Cedergren R. Gray M.W. Abel Y. Sankoff D. The evolutionary relationships among known life forms J. Mol. Evol. 1988 28 98 112 10.1007/BF02143501 3148747 · DOI
  8. [9]Gray M. Cedergren R. Abel Y. Sankoff D. On the evolutionary origin of the plant mitochondrion and its genome Proc. Natl. Acad. Sci. USA 1989 86 2267 2271 10.1073/pnas.86.7.2267 16594021 PMC286893 · DOI
  9. [10]Yang D. Oyaizu Y. Oyaizu H. Olsen G.J. Woese C.R. Mitochondrial origins Proc. Natl. Acad. Sci. USA 1985 82 4443 4447 10.1073/pnas.82.13.4443 3892535 PMC391117 · DOI
  10. [11]Andersson S. Kurland C. Ancient and recent horizontal transfer events: The origins of Mitochondria APMIS 1998 106 5 14 10.1111/j.1600-0463.1998.tb05641.x 9850675 · DOI
  11. [12]Andersson S.G. Kurland C.G. Reductive evolution of resident genomes Trends Microbiol. 1998 6 263 268 10.1016/S0966-842X(98)01312-2 9717214 · DOI
  12. [13]Andersson D.I. Hughes D. Muller’s ratchet decreases fitness of a DNA-based microbe Proc. Natl. Acad. Sci. USA 1996 93 906 907 10.1073/pnas.93.2.906 8570657 PMC40156 · DOI
  13. [14]Andersson G.E. Kurland C.G. An extreme codon preference strategy: Codon reassignment Mol. Biol. Evol. 1991 8 530 544 10.1093/oxfordjournals.molbev.a040666 1921708 · DOI
  14. [15]Andersson S.G. Kurland C.G. Origins of mitochondria and hydrogenases Curr. Opin. Microbiol. 1999 2 535 541 10.1016/S1369-5274(99)00013-2 10508728 · DOI
  15. [16]Berg O.G. Kurland C.G. Why Mitochondrial Genes are Most Often Found in Nuclei Mol. Biol. Evol. 2000 17 951 961 10.1093/oxfordjournals.molbev.a026376 10833202 · DOI
  16. [17]Karlberg O. Canback B. Kurland C.G. Andersson S.G. The dual origin of the yeast mitochondrial proteome Yeast 2000 17 170 187 10.1155/2000/597406 11025528 PMC2448374 · DOI
  17. [18]Kimura M. Rare variant alleles in the light of the neutral theory Mol. Biol. Evol. 1983 1 84 93 10.1093/oxfordjournals.molbev.a040305 6599962 · DOI
  18. [19]Kerr J.F. Wyllie A.H. Currie A.R. Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics Br. J. Cancer 1972 26 239 257 10.1038/bjc.1972.33 4561027 PMC2008650 · DOI
  19. [20]Kroemer G. Mitochondrial implication in apoptosis. Towards an endosymbiont hypothesis of apoptosis evolution Cell Death Differ. 1997 4 443 456 10.1038/sj.cdd.4400266 16465265 · DOI
  20. [21]Klim J. Gładki A. Kucharczyk R. Zielenkiewicz U. Kaczanowski S. Ancestral State Reconstruction of the Apoptosis Machinery in the Common Ancestor of Eukaryotes G3 Genes Genom. Genet. 2018 8 2121 2134 10.1534/g3.118.200295 29703784 PMC5982838 · DOI
  21. [22]Bar-Yaacov D. Blumberg A. Mishmar D. Mitochondrial-nuclear co-evolution and its effects on OXPHOS activity and regula-tion Biochim. Biophys. Acta. 2012 1819 1107 1111 10.1016/j.bbagrm.2011.10.008 22044624 · DOI
  22. [23]Barrientos A. Kenyon L. Moraes C.T. Human xenomitochondrial cybrids. Cellular models of mitochondrial complex I deficiency J. Biol. Chem. 1998 273 14210 14217 10.1074/jbc.273.23.14210 9603924 · DOI
  23. [24]Kenyon L. Moraes C.T. Expanding the functional human mitochondrial DNA database by the establishment of primate xenomitochondrial cybrids Proc. Natl. Acad. Sci. USA 1997 94 9131 9135 10.1073/pnas.94.17.9131 9256447 PMC23071 · DOI
  24. [26]Lane N. Martin W.F. The energetics of genome complexity Nature 2010 467 929 934 10.1038/nature09486 20962839 · DOI · Paper page
  25. [27]Martin W. Koonin E.V. Introns and the origin of nucleus-cytosol compartmentalization Nature 2006 440 41 45 10.1038/nature04531 16511485 · DOI
  26. [28]Mitchell P.J. Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism Nature 1961 191 144 148 10.1038/191144a0 13771349 · DOI · Paper page
  27. [29]Martinez-Reyes I. Chandel N.S. Mitochondrial TCA cycle metabolites control physiology and disease Nat. Commun. 2020 11 102 10.1038/s41467-019-13668-3 31900386 PMC6941980 · DOI · Paper page
  28. [30]Wirth C. Brandt U. Hunte C. Zickermann V. Structure and function of mitochondrial complex I Biochim. Biophys. Acta (BBA) Bioenerg. 2016 1857 902 914 10.1016/j.bbabio.2016.02.013 26921811 · DOI
  29. [31]Neupane P. Bhuju S. Thapa N. Bhattarai H.K. ATP Synthase: Structure, Function and Inhibition Biomol. Concepts 2019 10 1 10 10.1515/bmc-2019-0001 30888962 · DOI
  30. [32]Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system Annu. Rev. Biochem. 1985 54 1015 1069 10.1146/annurev.bi.54.070185.005055 2862839 · DOI
  31. [33]Schagger H. Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria EMBO J. 2000 19 1777 1783 10.1093/emboj/19.8.1777 10775262 PMC302020 · DOI · Paper page
  32. [34]Shinzawa-Itoh K. Shimomura H. Yanagisawa S. Shimada S. Takahashi R. Oosaki M. Ogura T. Tsukihara T. Purification of Active Respiratory Supercomplex from Bovine Heart Mitochondria Enables Functional Studies J. Biol. Chem. 2016 291 4178 4184 10.1074/jbc.M115.680553 26698328 PMC4759192 · DOI
  33. [35]Moreno-Sanchez R. Bravo C. Westerhoff H.V. Determining and understanding the control of flux. An illustration in submi-tochondrial particles of how to validate schemes of metabolic control Eur. J. Biochem. 1999 264 427 433 10.1046/j.1432-1327.1999.00621.x 10491087 · DOI
  34. [36]Bianchi C. Genova M.L. Castelli G.P. Lenaz G. The mitochondrial respiratory chain is partially organized in a super-complex assembly: Kinetic evidence using flux control analysis J. Biol. Chem. 2004 279 36562 36569 10.1074/jbc.M405135200 15205457 · DOI
  35. [38]Acin-Perez R. Bayona-Bafaluy M.P. Silva P.F. Loshuertos R.M. Pérez-Martos A. Bruno C. Moraes C.T. Enríquez J.A. Respiratory Complex III Is Required to Maintain Complex I in Mammalian Mitochondria Mol. Cell 2004 13 805 815 10.1016/S1097-2765(04)00124-8 15053874 PMC3164363 · DOI
  36. [39]Diaz F. Fukui H. Garcia S. Moraes C.T. Cytochrome c Oxidase Is Required for the Assembly/Stability of Respiratory Complex I in Mouse Fibroblasts Mol. Cell. Biol. 2006 26 4872 4881 10.1128/MCB.01767-05 16782876 PMC1489173 · DOI
  37. [40]Alkhaja A.K. Jans D.C. Nikolov M. Vukotic M. Lytovchenko O. Ludewig F. Schliebs W. Riedel D. Urlaub H. Jakobs S. MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization Mol. Biol. Cell 2012 23 247 257 10.1091/mbc.e11-09-0774 22114354 PMC3258170 · DOI
  38. [41]Hoppins S. Collins S.R. Cassidy-Stone A. Hummel E. DeVay R.M. Lackner L.L. Westermann B. Schuldiner M. Weissman J.S. Nunnari J. A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria J. Cell Biol. 2011 195 323 340 10.1083/jcb.201107053 21987634 PMC3198156 · DOI
  39. [42]Von der Malsburg K. Müller J.M. Bohnert M. Oeljeklaus S. Kwiatkowska P. Becker T. Loniewska-Lwowska A. Wiese S. Rao S. Milenkovic D. Dual role of mitofilin in mito-chondrial membrane organization and protein biogenesis Dev. Cell. 2011 21 694 707 10.1016/j.devcel.2011.08.026 21944719 · DOI
  40. [43]Barbot M. Jans D.C. Schulz C. Denkert N. Kroppen B. Hoppert M. Jakobs S. Meinecke M. Mic10 Oligomerizes to Bend Mitochondrial Inner Membranes at Cristae Junctions Cell Metab. 2015 21 756 763 10.1016/j.cmet.2015.04.006 25955211 · DOI
  41. [44]Bohnert M. Zerbes R.M. Davies K. Mühleip A. Rampelt H. Horvath S.E. Boenke T. Kram A. Perschil I. Veenhuis M. Central Role of Mic10 in the Mitochondrial Contact Site and Cristae Organizing System Cell Metab. 2015 21 747 755 10.1016/j.cmet.2015.04.007 25955210 · DOI
  42. [45]Davies K.M. Anselmi C. Wittig I. Faraldo-Gómez J.D. Kühlbrandt W. Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae Proc. Natl. Acad. Sci. USA 2012 109 13602 13607 10.1073/pnas.1204593109 22864911 PMC3427116 · DOI · Paper page
  43. [46]Strauss M. Hofhaus G. Schröder R.R. Kühlbrandt W. Dimer ribbons of ATP synthase shape the inner mitochondrial membrane EMBO J. 2008 27 1154 1160 10.1038/emboj.2008.35 18323778 PMC2323265 · DOI
  44. [47]Davies K. Strauss M. Daum B. Kief J.H. Osiewacz H.D. Rycovska A. Zickermann V. Kühlbrandt W. Macromolecular organization of ATP synthase and complex I in whole mitochondria Proc. Natl. Acad. Sci. USA 2011 108 14121 14126 10.1073/pnas.1103621108 21836051 PMC3161574 · DOI
  45. [48]Wilkens V. Kohl W. Busch K. Restricted diffusion of OXPHOS complexes in dynamic mitochondria delays their exchange between cristae and engenders a transitory mosaic distribution J. Cell Sci. 2013 126 103 116 10.1242/jcs.108852 23038773 · DOI
  46. [49]Hoppins S. Lackner L. Nunnari J. The Machines that Divide and Fuse Mitochondria Annu. Rev. Biochem. 2007 76 751 780 10.1146/annurev.biochem.76.071905.090048 17362197 · DOI · Paper page
  47. [50]Cogliati S. Frezza C. Soriano M.E. Varanita T. Quintana-Cabrera R. Corrado M. Cipolat S. Costa V. Casarin A. Gomes L.C. Mitochondrial Cristae Shape Determines Respiratory Chain Supercomplexes Assembly and Respiratory Efficiency Cell 2013 155 160 171 10.1016/j.cell.2013.08.032 24055366 PMC3790458 · DOI · Paper page
  48. [53]Shiba-Fukushima K. Arano T. Matsumoto G. Inoshita T. Yoshida S. Ishihama Y. Ryu K.-Y. Nukina N. Hattori N. Imai Y. Phosphorylation of Mitochondrial Polyubiquitin by PINK1 Promotes Parkin Mitochondrial Tethering PLoS Genet. 2014 10 e1004861 10.1371/journal.pgen.1004861 25474007 PMC4256268 · DOI
  49. [54]Kane L.A. Lazarou M. Fogel A.I. Li Y. Yamano K. Sarraf S. Banerjee S. Youle R.J. PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity J. Cell Biol. 2014 205 143 153 10.1083/jcb.201402104 24751536 PMC4003245 · DOI · Paper page
  50. [55]Koyano F. Okatsu K. Kosako H. Tamura Y. Go E. Kimura M. Kimura Y. Tsuchiya H. Yoshihara H. Hirokawa T. Ubiquitin is phosphorylated by PINK1 to activate parkin Nature 2014 510 162 166 10.1038/nature13392 24784582 · DOI · Paper page
  51. [56]Lazarou M. Sliter D.A. Kane L.A. Sarraf S. Wang C. Burman J.L. Sideris D.P. Fogel A.I. Youle R.J. The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy Nat. Cell Biol. 2015 524 309 314 10.1038/nature14893 PMC5018156 26266977 · DOI · Paper page
  52. [57]Johansen T. Lamark T. Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors J. Mol. Biol. 2020 432 80 103 10.1016/j.jmb.2019.07.016 31310766 · DOI
  53. [58]Kawai T. Akira S. TLR signaling Semin. Immunol. 2007 19 24 32 10.1016/j.smim.2006.12.004 17275323 · DOI
  54. [59]Hatada E.N. Krappmann D. Scheidereit C. NF-kappaB and the innate immune response Curr. Opin. Immunol. 2000 12 52 58 10.1016/S0952-7915(99)00050-3 10679399 · DOI
  55. [60]Seth R.B. Sun L. Ea C.K. Chen Z.J. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3 Cell 2005 122 669 682 10.1016/j.cell.2005.08.012 16125763 · DOI · Paper page
  56. [61]Xu L.G. Wang Y.Y. Han K.J. Li L.Y. Zhai Z. Shu H.B. VISA is an adapter protein required for virus-triggered IFN-beta signaling Mol Cell. 2005 19 727 740 10.1016/j.molcel.2005.08.014 16153868 · DOI
  57. [62]Meylan E. Curran J. Hofmann K. Moradpour D. Binder M. Bartenschlager R. Tschopp J. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus Nature 2005 437 1167 1172 10.1038/nature04193 16177806 · DOI · Paper page
  58. [64]Jiang F. Ramanathan A. Miller M.T. Tang G.-Q. Gale M. Patel S.S. Marcotrigiano J. Structural basis of RNA recognition and activation by innate immune receptor RIG-I Nature 2011 479 423 427 10.1038/nature10537 21947008 PMC3430514 · DOI
  59. [65]Hei L. Zhong J. Faculty Opinions recommendation of Laboratory of genetics and physiology 2 (LGP2) plays an essential role in hepatitis C virus infection-induced interferon responses Hepatology 2017 65 1478 1491 10.1002/hep.29050 28090671 · DOI
  60. [66]Uchikawa E. Lethier M. Malet H. Brunel J. Gerlier D. Cusack S. Structural Analysis of dsRNA Binding to Anti-viral Pattern Recognition Receptors LGP2 and MDA5 Mol. Cell 2016 62 586 602 10.1016/j.molcel.2016.04.021 27203181 PMC4885022 · DOI
  61. [67]Liu Y. Olagnier D. Lin R. Host and Viral Modulation of RIG-I-Mediated Antiviral Immunity Front. Immunol. 2016 7 662 10.3389/fimmu.2016.00662 28096803 PMC5206486 · DOI
  62. [68]Tait S. Green D.R. Mitochondria and cell signalling J. Cell Sci. 2012 125 807 815 10.1242/jcs.099234 22448037 PMC3311926 · DOI · Paper page
  63. [69]Biacchesi S. LeBerre M. Lamoureux A. Louise Y. Lauret E. Boudinot P. Breémont M. Mitochondrial Antiviral Signaling Protein Plays a Major Role in Induction of the Fish Innate Immune Response against RNA and DNA Viruses J. Virol. 2009 83 7815 7827 10.1128/JVI.00404-09 19474100 PMC2715792 · DOI
  64. [70]Vazquez C. Horner S.M. MAVS Coordination of Antiviral Innate Immunity J. Virol. 2015 89 6974 6977 10.1128/JVI.01918-14 25948741 PMC4473567 · DOI
  65. [71]Belgnaoui S.M. Paz S. Hiscott J. Orchestrating the interferon antiviral response through the mitochondrial antiviral signaling (MAVS) adapter Curr. Opin. Immunol. 2011 23 564 572 10.1016/j.coi.2011.08.001 21865020 · DOI
  66. [73]Koshiba T. Yasukawa K. Yanagi Y. Kawabata S.-I. Mitochondrial Membrane Potential Is Required for MAVS-Mediated Antiviral Signaling Sci. Signal. 2011 4 ra7 10.1126/scisignal.2001147 21285412 · DOI
  67. [74]Brand M.D. The sites and topology of mitochondrial superoxide production Exp. Gerontol. 2010 45 466 472 10.1016/j.exger.2010.01.003 20064600 PMC2879443 · DOI · Paper page
  68. [75]Jounai N. Takeshita F. Kobiyama K. Sawano A. Miyawaki A. Xin K.-Q. Ishii K. Kawai T. Akira S. Suzuki K. The Atg5 Atg12 conjugate associates with innate antiviral immune responses Proc. Natl. Acad. Sci. USA 2007 104 14050 14055 10.1073/pnas.0704014104 17709747 PMC1955809 · DOI
  69. [76]Tal M. Sasai M. Lee H.K. Yordy B. Shadel G.S. Iwasaki A. Absence of autophagy results in reactive oxygen species-dependent amplification of RLR signaling Proc. Natl. Acad. Sci. USA 2009 106 2770 2775 10.1073/pnas.0807694106 19196953 PMC2650341 · DOI
  70. [78]Arsenijevic D. Onuma H. Pecqueur C. Raimbault S. Manning B.S. Miroux B. Couplan E. Alves-Guerra M.-C. Goubern M. Surwit R. Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production Nat. Genet. 2000 26 435 439 10.1038/82565 11101840 · DOI
  71. [79]Rousset S. Emre Y. Join-Lambert O. Hurtaud C. Ricquier D. Cassard A.-M. The uncoupling protein 2 modulates the cytokine balance in innate immunity Cytokine 2006 35 135 142 10.1016/j.cyto.2006.07.012 16971137 · DOI · Paper page
  72. [80]Kizaki T. Suzuki K. Hitomi Y. Taniguchi N. Saitoh D. Watanabe K. Onoé K. Day N.K. Good R.A. Ohno H. Uncoupling protein 2 plays an important role in nitric oxide production of lipopolysaccharide-stimulated macrophages Proc. Natl. Acad. Sci. USA 2002 99 9392 9397 10.1073/pnas.142206299 12089332 PMC123151 · DOI
  73. [81]Geng J. Sun X. Wang P. Zhang S. Wang X. Wu H. Hong L. Xie C. Li X. Zhao H. Kinases Mst1 and Mst2 positively regulate phagocytic induction of reactive oxygen species and bactericidal activity Nat. Immunol. 2015 16 1142 1152 10.1038/ni.3268 26414765 PMC4618176 · DOI · Paper page
  74. [82]West A.P. Brodsky I.E. Rahner C. Woo D.K. Erdjument-Bromage H. Tempst P. Walsh M.C. Choi Y. Shadel G.S. Ghosh S. TLR signalling augments macrophage bactericidal activity through mitochondrial ROS Nature 2011 472 476 480 10.1038/nature09973 21525932 PMC3460538 · DOI · Paper page
  75. [84]Sahoo M. Ceballos-Olvera I. Del Barrio L. Re F. Role of the Inflammasome, IL-1β, and IL-18 in Bacterial Infections Sci. World J. 2011 11 2037 2050 10.1100/2011/212680 22125454 PMC3217589 · DOI
  76. [85]Liu X. Zhang Z. Ruan J. Pan Y. Magupalli V.G. Wu H. Lieberman J. Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores Nature 2016 535 153 158 10.1038/nature18629 27383986 PMC5539988 · DOI · Paper page
  77. [86]Bergsbaken T. Fink S. Cookson B.T. Pyroptosis: Host cell death and inflammation Nat. Rev. Genet. 2009 7 99 109 10.1038/nrmicro2070 PMC2910423 19148178 · DOI
  78. [87]Miao E.A. Rajan J.V. Aderem A. Caspase-1-induced pyroptotic cell death Immunol. Rev. 2011 243 206 214 10.1111/j.1600-065X.2011.01044.x 21884178 PMC3609431 · DOI
  79. [89]Hornung V. Latz E. Critical functions of priming and lysosomal damage for NLRP3 activation Eur. J. Immunol. 2010 40 620 623 10.1002/eji.200940185 20201015 PMC3893565 · DOI
  80. [90]Guarda G. Zenger M. Yazdi A.S. Schroder K. Ferrero I. Menu P. Tardivel A. Mattmann C. Tschopp J. Differential Expression of NLRP3 among Hematopoietic Cells J. Immunol. 2011 186 2529 2534 10.4049/jimmunol.1002720 21257968 · DOI
  81. [92]Davis B.K. Wen H. Ting J.P.-Y. The Inflammasome NLRs in Immunity, Inflammation, and Associated Diseases Annu. Rev. Immunol. 2011 29 707 735 10.1146/annurev-immunol-031210-101405 21219188 PMC4067317 · DOI · Paper page
  82. [93]Martinon F. Burns K. Tschopp J. The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta Mol. Cell. 2002 10 417 426 10.1016/S1097-2765(02)00599-3 12191486 · DOI · Paper page
  83. [94]Shi J. Zhao Y. Wang K. Shi X. Wang Y. Huang H. Zhuang Y. Cai T. Wang F. Shao F. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death Nature 2015 526 660 665 10.1038/nature15514 26375003 · DOI · Paper page
  84. [95]Subramanian N. Natarajan K. Clatworthy M.R. Wang Z. Germain R.N. The Adaptor MAVS Promotes NLRP3 Mitochondrial Localization and Inflammasome Activation Cell 2013 153 348 361 10.1016/j.cell.2013.02.054 23582325 PMC3632354 · DOI
  85. [96]Iyer S.S. He Q. Janczy J.R. Elliott E. Zhong Z. Olivier A.K. Sadler J.J. Knepper-Adrian V. Han R. Qiao L. Mitochondrial Cardiolipin Is Required for Nlrp3 Inflammasome Activation Immunity 2013 39 311 323 10.1016/j.immuni.2013.08.001 23954133 PMC3779285 · DOI
  86. [98]Abais J.M. Xia M. Zhang Y. Boini K.M. Li P.L. Redox regulation of NLRP3 inflammasomes: ROS as trigger or effector? Antioxid. Redox. Signal 2015 22 1111 1129 10.1089/ars.2014.5994 25330206 PMC4403231 · DOI
  87. [99]Kelley N. Jeltema D. Duan Y. He Y. The NLRP3 Inflammasome: An Overview of Mechanisms of Activation and Regulation Int. J. Mol. Sci. 2019 20 3328 10.3390/ijms20133328 PMC6651423 31284572 · DOI · Paper page
  88. [101]Riley J.S. Tait S.W. Mitochondrial DNA in inflammation and immunity EMBO Rep. 2020 21 e49799 10.15252/embr.201949799 32202065 PMC7132203 · DOI
  89. [102]West A.P. Khoury-Hanold W. Staron M. Tal M. Pineda C.M. Lang S.M. Bestwick M. Duguay B.A. Raimundo N. MacDuff D.A. Mitochondrial DNA stress primes the antiviral innate immune response Nature 2015 520 553 557 10.1038/nature14156 25642965 PMC4409480 · DOI · Paper page
  90. [103]Shimada K. Crother T. Karlin J. Dagvadorj J. Chiba N. Chen S. Ramanujan V.K. Wolf A.J. Vergnes L. Ojcius D. Oxidized Mitochondrial DNA Activates the NLRP3 Inflammasome during Apoptosis Immunity 2012 36 401 414 10.1016/j.immuni.2012.01.009 22342844 PMC3312986 · DOI · Paper page
  91. [105]Weinberg S. Sena L.A. Chandel N.S. Mitochondria in the Regulation of Innate and Adaptive Immunity Immunity 2015 42 406 417 10.1016/j.immuni.2015.02.002 25786173 PMC4365295 · DOI · Paper page
  92. [106]Escoll P. Mondino S. Rolando M. Buchrieser C. Targeting of host organelles by pathogenic bacteria: A sophisticated subversion strategy Nat. Rev. Genet. 2015 14 5 19 10.1038/nrmicro.2015.1 26594043 · DOI
  93. [107]Kramer T. Enquist L.W. Alphaherpesvirus infection disrupts mitochondrial transport in neurons Cell Host Microbe 2012 11 504 514 10.1016/j.chom.2012.03.005 22607803 PMC3358700 · DOI
  94. [108]Chatel-Chaix L. Cortese M. Brey I.R. Bender S. Neufeldt C. Fischl W. Scaturro P. Schieber N. Schwab Y. Fischer B. Dengue Virus Perturbs Mitochondrial Morphodynamics to Dampen Innate Immune Responses Cell Host Microbe 2016 20 342 356 10.1016/j.chom.2016.07.008 27545046 PMC7105029 · DOI
  95. [109]Gilardini Montani M.S. Santarelli R. Granato M. Gonnella R. Torrisi M.R. Faggioni A.; Cirone, M. EBV reduces autophagy, intracellular ROS and mitochondria to impair monocyte survival and differentiation Autophagy 2019 15 652 667 10.1080/15548627.2018.1536530 30324853 PMC6526866 · DOI
  96. [110]Wang L.W. Shen H. Nobre L. Ersing I. Paulo J.A. Trudeau S. Wang Z. Smith N.A. Ma Y. Reinstadler B. Epstein-Barr-Virus-Induced One-Carbon Metabolism Drives B Cell Transformation Cell Metab. 2019 30 539 555 10.1016/j.cmet.2019.06.003 31257153 PMC6720460 · DOI · Paper page
  97. [111]Song S. Jiang Z. Spezia-Lindner D.E. Liang T. Xu C. Wang H. Tian Y. Bai Y. BHRF1 Enhances EBV Mediated Nasopharyngeal Carcinoma Tumorigenesis through Modulating Mitophagy Associated with Mitochondrial Membrane Permeabilization Transition Cells 2020 9 1158 10.3390/cells9051158 32392902 PMC7290790 · DOI
  98. [112]Kim S.-J. Khan M. Quan J. Till A. Subramani S. Siddiqui A. Hepatitis B Virus Disrupts Mitochondrial Dynamics: Induces Fission and Mitophagy to Attenuate Apoptosis PLoS Pathog. 2013 9 e1003722 10.1371/journal.ppat.1003722 24339771 PMC3855539 · DOI
  99. [113]Kim S.-J. Syed G. Siddiqui A. Hepatitis C Virus Induces the Mitochondrial Translocation of Parkin and Subsequent Mitophagy PLoS Pathog. 2013 9 e1003285 10.1371/journal.ppat.1003285 23555273 PMC3610669 · DOI
  100. [114]Day E.A. O’Neill L.A.J. Targeting mitochondria to beat HIV-1 Nat. Immunol. 2021 22 1 2 10.1038/s41590-021-00881-w 33767428 · DOI
  101. [115]Wang S.F. Tseng S.P. Huang S.W. Yen C.H. Hong Y.W. Chen M. Chen Y.M.A. Mitochondria polarization in the contact regions of vi-rus-infected effector cells during cell-to-cell transmission of HIV-1 AIDS Res. Hum. Retrovir. 2015 31 175 176 10.1089/aid.2014.0328 25680076 PMC4313420 · DOI
  102. [116]Teodorof-Diedrich C. Spector S.A. Human Immunodeficiency Virus Type 1 gp120 and Tat Induce Mitochondrial Fragmenta-tion and Incomplete Mitophagy in Human Neurons J. Virol. 2018 92 22 10.1128/JVI.00993-18 PMC6206485 30158296 · DOI
  103. [117]Al-Mehdi A.-B. Pastukh V.V. Swiger B.M. Reed D.J. Patel M.R. Bardwell G.C. Alexeyev M.F. Gillespie M.N. Perinuclear Mitochondrial Clustering Creates an Oxidant-Rich Nuclear Domain Required for Hypoxia-Induced Transcription Sci. Signal. 2012 5 ra47 10.1126/scisignal.2002712 22763339 PMC3565837 · DOI
  104. [119]Wang R. Zhu Y. Lin X. Ren C. Zhao J. Wang F. Gao X. Xiao R. Zhao L. Chen H. Influenza M2 protein regulates MAVS-mediated signaling pathway through interacting with MAVS and increasing ROS production Autophagy 2019 15 1163 1181 10.1080/15548627.2019.1580089 30741586 PMC6613841 · DOI
  105. [120]Shi C.S. Qi H.Y. Boularan C. Huang N.N. Abu-Asab M. Shelhamer J.H. Kehrl J.H. SARS-coronavirus open reading frame-9b sup-presses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome J. Immunol. 2014 193 3080 3089 10.4049/jimmunol.1303196 25135833 PMC4179872 · DOI
  106. [121]Jiang H. Gong T. Zhou R. The strategies of targeting the NLRP3 inflammasome to treat inflammatory diseases Adv. Immunol. 2020 145 55 93 32081200
  107. [122]Mehrzadi S. Karimi M.Y. Fatemi A. Reiter R.J. Hosseinzadeh A. SARS-CoV-2 and other coronaviruses negatively influence mitochondrial quality control: Beneficial effects of melatonin Pharmacol. Ther. 2021 224 107825 10.1016/j.pharmthera.2021.107825 33662449 PMC7919585 · DOI
  108. [123]Singh K. Chen Y.C. Hassanzadeh S. Han K. Judy J.T. Seifuddin F. Tunc I. Sack M.N. Pirooznia M. Network Analysis and Transcriptome Profiling Identify Autophagic and Mitochondrial Dysfunctions in SARS-CoV-2 Infection Front. Genet. 2021 12 289 10.3389/fgene.2021.599261 PMC8008150 33796130 · DOI
  109. [124]Andargie T.E. Tsuji N. Seifuddin F. Jang M.K. Yuen P.S. Kong H. Tunc I. Singh K. Charya A. Wilkins K.J. Cell-free DNA maps COVID-19 tissue injury and risk of death and can cause tissue injury JCI Insight 2021 6 7 10.1172/jci.insight.147610 33651717 PMC8119224 · DOI
  110. [125]Michi A.N. Yipp B.G. Dufour A. Lopes F. Proud D. PGC-1α mediates a metabolic host defense response in human airway epithelium during rhinovirus infections Nat. Commun. 2021 12 1 19 10.1038/s41467-021-23925-z 34135327 PMC8209127 · DOI
  111. [126]Lai D. Tan C.L. Gunaratne J. Quek L.S. Nei W.L. Thierry F. Bellanger S. Localization of HPV-18 E2 at Mitochondrial Membranes Induces ROS Release and Modulates Host Cell Metabolism PLoS ONE 2013 8 e75625 10.1371/journal.pone.0075625 24086592 PMC3782431 · DOI
  112. [127]Raj K. Berguerand S. Southern S. Doorbar J. Beard P. E1 empty set E4 protein of human papillomavirus type 16 associates with mitochondria J. Virol. 2004 78 7199 7207 10.1128/JVI.78.13.7199-7207.2004 15194796 PMC421641 · DOI
  113. [128]Cruz-Gregorio A. Manzo-Merino J. Gonzaléz-García M.C. Pedraza-Chaverri J. Medina-Campos O.N. Valverde M. Rojas E. Rodríguez-Sastre M.A. Garcia-Cuellar C.M. Lizano M. Human Papillomavirus Types 16 and 18 Early-expressed Proteins Differentially Modulate the Cellular Redox State and DNA Damage Int. J. Biol. Sci. 2018 14 21 35 10.7150/ijbs.21547 29483822 PMC5821046 · DOI
  114. [129]Keller A.C. Badani H. McClatchey P.M. Baird N.L. Bowlin J.L. Bouchard R. Perng O. Reusch J.E.B. Kaufer B.B. Gilden D. Varicella zoster virus infection of human fetal lung cells alters mitochondrial morphology J. Neuro Virol. 2016 22 674 682 10.1007/s13365-016-0457-0 PMC5480379 27245593 · DOI
  115. [130]Gogvadze V. Zhivotovsky B. Orrenius S. The Warburg effect and mitochondrial stability in cancer cells Mol. Asp. Med. 2010 31 60 74 10.1016/j.mam.2009.12.004 19995572 · DOI
  116. [131]Liu X. Li Q. Dowdell K. Fischer E.R. Cohen J.I. Varicella-Zoster virus ORF12 protein triggers phosphorylation of ERK1/2 and inhibits apoptosis J. Virol. 2012 86 3143 3151 10.1128/JVI.06923-11 22238304 PMC3302337 · DOI
  117. [132]Carvalho F. Spier A. Chaze T. Matondo M. Cossart P. Stavru F. Listeria monocytogenes Exploits Mitochondrial Contact Site and Cristae Organizing System Complex Subunit Mic10 To Promote Mitochondrial Fragmentation and Cellular Infection mBio 2020 11 10.1128/mBio.03171-19 32019800 PMC7002346 · DOI
  118. [133]Stavru F. Bouillaud F. Sartori A. Ricquier D. Cossart P. Listeria monocytogenes transiently alters mitochondrial dynamics during infection Proc. Natl. Acad. Sci. USA 2011 108 3167 3612 10.1073/pnas.1100126108 21321208 PMC3048117 · DOI
  119. [134]Stavru F. Palmer A.E. Wang C. Youle R.J. Cossart P. Atypical mitochondrial fission upon bacterial infection Proc. Natl. Acad. Sci. USA 2013 110 16003 16008 10.1073/pnas.1315784110 24043775 PMC3791707 · DOI
  120. [135]Escoll P. Song O.-R. Viana F. Steiner B. Lagache T. Olivo-Marin J.-C. Impens F. Brodin P. Hilbi H. Buchrieser C. Legionella pneumophila Modulates Mitochondrial Dynamics to Trigger Metabolic Repurposing of Infected Macrophages Cell Host Microbe 2017 22 302 316 10.1016/j.chom.2017.07.020 28867389 · DOI
  121. [136]Chowdhury S.R. Reimer A. Sharan M. Kozjak-Pavlovic V. Eulalio A. Prusty B.K. Fraunholz M. Karunakaran K. Rudel T. Chlamydia preserves the mitochondrial network necessary for replication via microRNA-dependent inhibition of fission J. Cell Biol. 2017 216 1071 1089 10.1083/jcb.201608063 28330939 PMC5379946 · DOI
  122. [137]Abdul-Sater A.A. Saïd-Sadier N. Lam V.M. Singh B. Pettengill M.A. Soares F. Tattoli I. Lipinski S. Girardin S.E. Rosenstiel P. Enhancement of Reactive Oxygen Species Production and Chlamydial Infection by the Mitochondrial Nod-like Family Member NLRX1 J. Biol. Chem. 2010 285 41637 41645 10.1074/jbc.M110.137885 20959452 PMC3009891 · DOI
  123. [138]Boncompain G. Schneider B. Delevoye C. Kellermann O. Dautry-Varsat A. Subtil A. Production of Reactive Oxygen Species Is Turned on and Rapidly Shut Down in Epithelial Cells Infected with Chlamydia trachomatis Infect. Immun. 2010 78 80 87 10.1128/IAI.00725-09 19858301 PMC2798218 · DOI
  124. [139]Jain P. Luo Z.Q. Blanke S.R. Helicobacter pylori vacuolating cytotoxin A (VacA) engages the mitochondrial fission machinery to induce host cell death Proc. Natl. Acad. Sci. USA 2011 108 16032 16037 10.1073/pnas.1105175108 21903925 PMC3179038 · DOI
  125. [140]Lum M. Morona R. Dynamin-related protein Drp1 and mitochondria are important for Shigella flexneri infection Int. J. Med. Microbiol. 2014 304 530 541 10.1016/j.ijmm.2014.03.006 24755420 · DOI
  126. [141]Sirianni A. Krokowski S. Lobato-Márquez D. Buranyi S. Pfanzelter J. Galea D. Willis A. Culley S. Henriques R. Larrouy-Maumus G. Mitochondria mediate septin cage as-sembly to promote autophagy of Shigella EMBO Rep. 2016 17 1029 1043 10.15252/embr.201541832 27259462 PMC4931556 · DOI
  127. [142]Chen M. Gan H. Remold H.G. A mechanism of virulence: Virulent Mycobacterium tuberculosis strain H37Rv, but not at-tenuated H37Ra, causes significant mitochondrial inner membrane disruption in macrophages leading to necrosis J Immunol. 2006 176 3707 3716 10.4049/jimmunol.176.6.3707 16517739 · DOI · Paper page
  128. [143]Jamwal S. Midha M.K. Verma H.N. Basu A. Rao K.V. Manivel V. Characterizing virulence-specific perturbations in the mito-chondrial function of macrophages infected with Mycobacterium tuberculosis Sci. Rep. 2013 3 1328 10.1038/srep01328 23435464 PMC3580321 · DOI
  129. [144]Vyatkina G. Bhatia V. Gerstner A. Papaconstantinou J. Garg N. Impaired mitochondrial respiratory chain and bioenergetics during chagasic cardiomyopathy development Biochim. et Biophys. Acta (BBA) Mol. Basis Dis. 2004 1689 162 173 10.1016/j.bbadis.2004.03.005 15196597 · DOI
  130. [145]Wen J. Yachelini P.C. Sembaj A. Manzur R.E. Garg N.J. Increased oxidative stress is correlated with mitochondrial dysfunction in chagasic patients Free. Radic. Biol. Med. 2006 41 270 276 10.1016/j.freeradbiomed.2006.04.009 16814107 · DOI
  131. [146]Gupta S. Wen J.J. Garg N.J. Oxidative stress in Chagas disease Interdiscip. Perspect. Infect. Dis. 2009 2009 190354 10.1155/2009/190354 19547716 PMC2696642 · DOI
  132. [147]Wen J.-J. Garg N. Oxidative modification of mitochondrial respiratory complexes in response to the stress of Trypanosoma cruzi infection Free. Radic. Biol. Med. 2004 37 2072 2081 10.1016/j.freeradbiomed.2004.09.011 15544925 · DOI
  133. [148]Rojas Marquez J.D. Ana Y. Baigorri R.E. Stempin C.C. Cerban F.M. Mammalian Target of Rapamycin Inhibition in Trypanosoma cruzi-Infected Macrophages Leads to an Intracellular Profile That Is Detrimental for Infection Front. Immunol. 2018 9 313 10.3389/fimmu.2018.00313 29515594 PMC5826284 · DOI
  134. [149]Wan X. Gupta S. Zago M.P. Davidson M.M. Dousset P. Amoroso A. Garg N.J. Defects of mtDNA replication impaired mitochondrial biogenesis during Trypanosoma cruzi infection in human cardiomyocytes and chagasic patients: The role of Nrf1/2 and anti-oxidant response J. Am. Heart. Assoc. 2012 1 e003855 10.1161/JAHA.112.003855 23316324 PMC3540675 · DOI
  135. [150]Wen J.J. Yin Y.W. Garg N.J. PARP1 depletion improves mitochondrial and heart function in Chagas disease: Effects on POLG dependent mtDNA maintenance PLoS Pathog. 2018 14 e1007065 10.1371/journal.ppat.1007065 29851986 PMC5979003 · DOI
  136. [151]Gupta S. Bhatia V. Wen J.-J. Wu Y. Huang M.-H. Garg N.J. Trypanosoma cruzi infection disturbs mitochondrial membrane potential and ROS production rate in cardiomyocytes Free. Radic. Biol. Med. 2009 47 1414 1421 10.1016/j.freeradbiomed.2009.08.008 19686837 PMC2767388 · DOI
  137. [152]Wen J.J. Dhiman M. Whorton E.B. Garg N.J. Tissue-specific oxidative imbalance and mitochondrial dysfunction during Trypa-nosoma cruzi infection in mice Microbes Infect. 2008 10 1201 1209 10.1016/j.micinf.2008.06.013 18675934 PMC2613841 · DOI
  138. [153]Gonzalez-Ortiz L.M. Sanchez-Villamil J.P. Celis-Rodriguez M.A. Lineros G. Sanabria-Barrera S. Serrano N.C. Rincon M.Y. Bautista-Nino P.K. Measuring mitochondrial respiration in adherent cells infected with Trypanosoma cruzi Chagas, 1909 using Seahorse extracellular flux analyser Folia Parasitol. 2019 66 1 9 10.14411/fp.2019.016 31631068 · DOI
  139. [154]Shivappagowdar A. Garg S. Srivastava A. Hada R. Kalia I. Singh A. Garg L. Pati S. Singh S. Pathogenic Pore Forming Proteins of Plasmodium Triggers the Necrosis of Endothelial Cells Attributed to Malaria Severity Toxins 2021 13 62 10.3390/toxins13010062 33467515 PMC7839052 · DOI
  140. [155]Kaushansky A. Metzger P.G. Douglass A.N. Mikolajczak S.A. Lakshmanan V. Kain H.S. Kappe S.H. Malaria parasite liver stages render host hepatocytes susceptible to mitochondria-initiated apoptosis Cell Death Dis. 2013 4 e762 10.1038/cddis.2013.286 23928701 PMC3763448 · DOI
  141. [156]Kaushansky A. Ye A.S. Austin L.S. Mikolajczak S. Vaughan A.M. Camargo N. Metzger P.G. Douglass A.N. MacBeath G. Kappe S.H. Suppression of Host p53 Is Critical for Plasmodium Liver-Stage Infection Cell Rep. 2013 3 630 637 10.1016/j.celrep.2013.02.010 23478020 PMC3619000 · DOI
  142. [157]Martinou J.-C. Youle R.J. Mitochondria in Apoptosis: Bcl-2 Family Members and Mitochondrial Dynamics Dev. Cell 2011 21 92 101 10.1016/j.devcel.2011.06.017 21763611 PMC3156409 · DOI
  143. [158]Syn G. Anderson D. Blackwell J.M. Jamieson S.E. Toxoplasma gondii Infection Is Associated with Mitochondrial Dysfunction in-Vitro Front. Cell. Infect. Microbiol. 2017 7 512 10.3389/fcimb.2017.00512 29312892 PMC5733060 · DOI
  144. [159]Pernas L. Bean C. Boothroyd J.C. Scorrano L. Mitochondria Restrict Growth of the Intracellular Parasite Toxoplasma gondii by Limiting Its Uptake of Fatty Acids Cell Metab. 2018 27 886 897.e4 10.1016/j.cmet.2018.02.018 29617646 · DOI · Paper page
  145. [160]Blader I.J. Manger I.D. Boothroyd J.C. Microarray Analysis Reveals Previously Unknown Changes in Toxoplasma gondii-infected Human Cells J. Biol. Chem. 2001 276 24223 24231 10.1074/jbc.M100951200 11294868 · DOI
  146. [161]He J.-J. Ma J. Li F.-C. Song H.-Q. Xu M.-J. Zhu X.-Q. Transcriptional changes of mouse splenocyte organelle components following acute infection with Toxoplasma gondii Exp. Parasitol. 2016 167 7 16 10.1016/j.exppara.2016.04.019 27132051 · DOI
  147. [162]Chakrabarty Y. Bhattacharyya S.N. Leishmania donovani restricts mitochondrial dynamics to enhance miRNP stability and target RNA repression in host macrophages Mol. Biol. Cell. 2017 28 2091 2105 10.1091/mbc.e16-06-0388 28539410 PMC5509422 · DOI
  148. [163]Moreira D. Rodrigues V. Abengozar M. Rivas L. Rial E. Laforge M. Li X. Foretz M. Viollet B. Estaquier J. Leishmania infantum Modulates Host Macrophage Mitochondrial Metabolism by Hijacking the SIRT1-AMPK Axis PLoS Pathog. 2015 11 e1004684 10.1371/journal.ppat.1004684 25738568 PMC4349736 · DOI
  149. [164]Eisenreich W. Rudel T. Heesemann J. Goebel W. How Viral and Intracellular Bacterial Pathogens Reprogram the Metabolism of Host Cells to Allow Their Intracellular Replication Front. Cell. Infect. Microbiol. 2019 9 42 10.3389/fcimb.2019.00042 30886834 PMC6409310 · DOI
  150. [165]Cruz-Gregorio A. Aranda-Rivera A.K. Pedraza-Chaverri J. Human Papillomavirus-related Cancers and Mitochondria Virus Res. 2020 286 198016 10.1016/j.virusres.2020.198016 32445871 · DOI
  151. [166]Kim Y.R. Kim J.S. Yun J.S. Kim S. Kim S.Y. Jang K. Yang C.S. Toxoplasma gondii GRA8 induces ATP5A1-SIRT3-mediated mito-chondrial metabolic resuscitation: A potential therapy for sepsis Exp. Mol. Med. 2018 50 e464 10.1038/emm.2017.308 29869623 PMC5898902 · DOI
  152. [167]Dustin M.L. The immunological synapse Cancer Immunol. Res. 2014 2 1023 1033 10.1158/2326-6066.CIR-14-0161 25367977 PMC4692051 · DOI · Paper page
  153. [168]Jiang H.W. Zhang H.N. Meng Q.F. Xie J. Li Y. Chen H. Zheng Y.X. Wang X.N. Qi H. Zhang J. SARS-CoV-2 Orf9b suppresses type I interferon responses by targeting TOM70 Cell Mol. Immunol. 2020 17 998 1000 10.1038/s41423-020-0514-8 32728199 PMC7387808 · DOI · Paper page
  154. [169]Kalashnyk O. Lykhmus O. Izmailov M. Koval L. Komisarenko S. Skok M. SARS-Cov-2 spike protein fragment 674–685 protects mitochondria from releasing cytochrome c in response to apoptogenic influence Biochem. Biophys. Res. Commun. 2021 561 14 18 10.1016/j.bbrc.2021.05.018 34000512 PMC8112323 · DOI
  155. [170]Flannagan R.S. Cosío G. Grinstein S. Antimicrobial mechanisms of phagocytes and bacterial evasion strategies Nat. Rev. Genet. 2009 7 355 366 10.1038/nrmicro2128 19369951 · DOI · Paper page
  156. [171]Spier A. Stavru F. Cossart P. Interaction between Intracellular Bacterial Pathogens and Host Cell Mitochondria Microbiol. Spectr. 2019 7 2 10.1128/microbiolspec.BAI-0016-2019 30848238 PMC11590420 · DOI
  157. [172]Mohareer K. Medikonda J. Vadankula G.R. Banerjee S. Mycobacterial Control of Host Mitochondria: Bioenergetic and Metabolic Changes Shaping Cell Fate and Infection Outcome Front. Cell. Infect. Microbiol. 2020 10 457 10.3389/fcimb.2020.00457 33102245 PMC7554303 · DOI
  158. [173]Lee K. Choi S. Choi H. Gurmessa S.K. Dang T.B. Back Y.W. Park H. Kim H. Recombinant Rv1654 protein of Mycobacterium tuberculosis induces mitochondria-mediated apoptosis in macrophage Microbiol. Immunol. 2021 65 178 188 10.1111/1348-0421.12880 33565648 · DOI
  159. [174]Voleman L. Dolezal P. Mitochondrial dynamics in parasitic protists PLoS Pathog. 2019 15 e1008008 10.1371/journal.ppat.1008008 31751405 PMC6871780 · DOI
  160. [175]Cunha-Neto E. Chevillard C. Chagas disease cardiomyopathy: Immunopathology and genetics Mediators Inflamm. 2014 2014 683230 10.1155/2014/683230 25210230 PMC4152981 · DOI
  161. [176]Da Silveira A.B.M. Lemos E.M. Adad S.J. Correa-Oliveira R. Furness J.B. Reis D.D.A. Megacolon in Chagas disease: A study of inflammatory cells, enteric nerves, and glial cells Hum. Pathol. 2007 38 1256 1264 10.1016/j.humpath.2007.01.020 17490721 · DOI
  162. [177]Paiva C.N. Medei E. Bozza M.T. ROS and Trypanosoma cruzi: Fuel to infection, poison to the heart PLoS Pathog. 2018 14 e1006928 10.1371/journal.ppat.1006928 29672619 PMC5908069 · DOI
  163. [178]Milduberger N. Bustos P.L. González C. Perrone A.E. Postan M. Bua J. Trypanosoma cruzi infection in Cyclophilin D deficient mice Exp. Parasitol. 2020 220 108044 10.1016/j.exppara.2020.108044 33253715 · DOI
  164. [179]Hossain E. Khanam S. Dean D.A. Wu C. Lostracco-Johnson S. Thomas D. Kane S.S. Parab A.R. Flores K. Katemauswa M. Mapping of host-parasite-microbiome inter-actions reveals metabolic determinants of tropism and tolerance in Chagas disease Sci. Adv. 2020 6 eaaz2015 10.1126/sciadv.aaz2015 32766448 PMC7385396 · DOI
  165. [180]Liu Z. Ulrich vonBargen R. McCall L.I. Central role of metabolism in Trypanosoma cruzi tropism and Chagas disease patho-genesis Curr. Opin. Microbiol. 2021 63 204 229 10.1016/j.mib.2021.07.015 34455304 PMC8463485 · DOI
  166. [181]Subauste C.S. Recent Advances in the Roles of Autophagy and Autophagy Proteins in Host Cells During Toxoplasma gondii Infection and Potential Therapeutic Implications Front. Cell Dev. Biol. 2021 9 10.3389/fcell.2021.673813 PMC8220159 34179003 · DOI
  167. [182]Pernas L. Adomako-Ankomah Y. Shastri A.J. Ewald S.E. Treeck M. Boyle J.P. Boothroyd J.C. Toxoplasma effector MAF1 mediates re-cruitment of host mitochondria and impacts the host response PLoS Biol. 2014 12 e1001845 10.1371/journal.pbio.1001845 24781109 PMC4004538 · DOI
  168. [183]Nelson M.M. Jones A.R. Carmen J.C. Sinai A.P. Burchmore R. Wastling J.M. Modulation of the host cell proteome by the intra-cellular apicomplexan parasite Toxoplasma gondii Infect. Immun. 2008 76 828 844 10.1128/IAI.01115-07 17967855 PMC2223483 · DOI
  169. [184]Blank M.L. Xia J. Morcos M.M. Sun M. Cantrell P.S. Liu Y. Zeng X. Powell C.J. Yates N. Boulanger M.J. Toxoplasma gondii association with host mitochondria requires key mitochondrial protein import machinery Proc. Natl. Acad. Sci. USA 2021 118 e2013336118 10.1073/pnas.2013336118 33723040 PMC7999873 · DOI
  170. [185]Su X.-Z. Zhang C. Joy D.A. Host-Malaria Parasite Interactions and Impacts on Mutual Evolution Front. Cell. Infect. Microbiol. 2020 10 587933 10.3389/fcimb.2020.587933 33194831 PMC7652737 · DOI
  171. [186]Scarpelli P.H. Pecenin M.F. Garcia C.R.S. Intracellular Ca2+ Signaling in Protozoan Parasites: An Overview with a Focus on Mitochondria Int. J. Mol. Sci. 2021 22 469 10.3390/ijms22010469 PMC7796463 33466510 · DOI
  172. [187]Ryan M.T. Hoogenraad N.J. Mitochondrial-Nuclear Communications Annu. Rev. Biochem. 2007 76 701 722 10.1146/annurev.biochem.76.052305.091720 17227225 · DOI · Paper page
  173. [188]Soledad R.B. Charles S. Samarjit D. The secret messages between mitochondria and nucleus in muscle cell biology Arch. Biochem. Biophys. 2019 666 52 62 10.1016/j.abb.2019.03.019 30935885 PMC6538274 · DOI
  174. [189]Rius-Pérez S. Torres-Cuevas I. Millán I. Ortega Á.L. Pérez S. PGC-1alpha, Inflammation, and Oxidative Stress: An Integrative View in Metabolism Oxid. Med. Cell Longev. 2020 2020 1452696 10.1155/2020/1452696 32215168 PMC7085407 · DOI
  175. [190]Xiong S. Patrushev N. Forouzandeh F. Hilenski L. Alexander R.W. PGC-1α Modulates Telomere Function and DNA Damage in Protecting against Aging-Related Chronic Diseases Cell Rep. 2015 12 1391 1399 10.1016/j.celrep.2015.07.047 26299964 PMC4549794 · DOI
  176. [191]Leone T.C. Lehman J.J. Finck B.N. Schaeffer P.J. Wende A.R. Boudina S. Courtois M. Wozniak D.F. Sambandam N. Bernal-Mizrachi C. PGC-1alpha deficiency causes multi-system energy metabolic derangements: Muscle dysfunction, abnormal weight control and hepatic steatosis PLoS Biol. 2005 3 e101 10.1371/journal.pbio.0030101 15760270 PMC1064854 · DOI · Paper page
  177. [192]Fontecha-Barriuso M. Martín-Sánchez D. Martinez-Moreno J.M. Carrasco S. Ruiz-Andrés O. Monsalve M. Sanchez-Ramos C. Gómez M.J. Ruiz-Ortega M. Sánchez-Niño M.D. PGC-1alpha deficiency causes spontaneous kidney inflammation and increases the severity of nephrotoxic AKI J. Pathol. 2019 249 65 78 10.1002/path.5282 30982966 · DOI
  178. [193]Chambers K.T. Chen Z. Crawford P. Fu X. Burgess S.C. Lai L. Leone T.C. Kelly D.P. Finck B.N. Liver-Specific PGC-1beta Deficiency Leads to Impaired Mitochondrial Function and Lipogenic Response to Fasting-Refeeding PLoS ONE 2012 7 e52645 10.1371/journal.pone.0052645 23285128 PMC3532159 · DOI
  179. [194]Bloise F.F. Santos A.T. de Brito J. de Andrade C.B.V. Oliveira T.S. de Souza A.F.P. Fontes K.N. Silva J.D. Blanco N. Silva P.L. Sepsis Impairs Thyroid Hormone Signaling and Mitochondrial Function in the Mouse Diaphragm Thyroid 2020 30 1079 1090 10.1089/thy.2019.0124 32200709 · DOI
  180. [195]Suliman H.B. Welty-Wolf K.E. Carraway M. Tatro L. Piantadosi C.A. Piantadosi CA. Lipopolysaccharide induces oxidative cardiac mitochon-drial damage and biogenesis Cardiovasc. Res. 2004 64 279 288 10.1016/j.cardiores.2004.07.005 15485687 · DOI
  181. [196]Tzika A.A. Constantinou C. Bandyopadhaya A. Psychogios N. Lee S. Mindrinos M. Martyn J.A.J. Tompkins R.G. Rahme L.G. A Small Volatile Bacterial Molecule Triggers Mitochondrial Dysfunction in Murine Skeletal Muscle PLoS ONE 2013 8 e74528 10.1371/journal.pone.0074528 24098655 PMC3787027 · DOI
  182. [197]Herzig S. Shaw R.J. AMPK: Guardian of metabolism and mitochondrial homeostasis Nat. Rev. Mol. Cell Biol. 2018 19 121 135 10.1038/nrm.2017.95 28974774 PMC5780224 · DOI
  183. [198]Yang C.-S. Kim J.-J. Lee H.-M. Jin H.S. Lee S.-H. Park J.-H. Kim S.J. Kim J.-M. Han Y.-M. Lee M.-S. The AMPK-PPARGC1A pathway is required for antimicrobial host defense through activation of autophagy Autophagy 2014 10 785 802 10.4161/auto.28072 24598403 PMC5119058 · DOI · Paper page
  184. [199]Gureev A.P. Shaforostova E.A. Popov V. Regulation of Mitochondrial Biogenesis as a Way for Active Longevity: Interaction Between the Nrf2 and PGC-1α Signaling Pathways Front. Genet. 2019 10 435 10.3389/fgene.2019.00435 31139208 PMC6527603 · DOI
  185. [200]Piantadosi C.A. Suliman H.B. Mitochondrial Transcription Factor A Induction by Redox Activation of Nuclear Respiratory Factor 1 J. Biol. Chem. 2006 281 324 333 10.1074/jbc.M508805200 16230352 · DOI
  186. [201]Scarpulla R.C. Vega R.B. Kelly D.P. Transcriptional integration of mitochondrial biogenesis Trends Endocrinol. Metab. 2012 23 459 466 10.1016/j.tem.2012.06.006 22817841 PMC3580164 · DOI · Paper page
  187. [202]Olagnier D. Peri S. Steel C. Van Montfoort N. Chiang C. Beljanski V. Slifker M. He Z. Nichols C.N. Lin R. Cellular Oxidative Stress Response Controls the Antiviral and Apoptotic Programs in Dengue Virus-Infected Dendritic Cells PLoS Pathog. 2014 10 e1004566 10.1371/journal.ppat.1004566 25521078 PMC4270780 · DOI
  188. [203]Ferrari M. Zevini A. Palermo E. Muscolini M. Alexandridi M. Etna M.P. Coccia E.M. Fernandez-Sesma A. Coyne C. Zhang D.D. Dengue Virus Targets Nrf2 for NS2B3-Mediated Degradation Leading to Enhanced Oxidative Stress and Viral Replication J. Virol. 2020 94 10.1128/JVI.01551-20 32999020 PMC7925186 · DOI
  189. [204]Fan X. Murray S.C. Staitieh B.S. Spearman P. Guidot D.M. HIV Impairs Alveolar Macrophage Function via Mi-croRNA-144-Induced Suppression of Nrf2 Am. J. Med. Sci. 2021 361 90 97 10.1016/j.amjms.2020.07.026 32773107 PMC7854972 · DOI · Paper page
  190. [205]Staitieh B.S. Ding L. Neveu W.A. Spearman P. Guidot D.M. Fan X. HIV-1 decreases Nrf2/ARE activity and phagocytic function in alveolar macrophages J. Leukoc. Biol. 2017 102 517 525 10.1189/jlb.4A0616-282RR 28550120 PMC5505750 · DOI
  191. [206]Wyler E. Franke V. Menegatti J. Kocks C. Boltengagen A. Praktiknjo S. Walch-Rückheim B. Bosse J. Rajewsky N. Grässer F. Single-cell RNA-sequencing of herpes simplex virus 1-infected cells connects NRF2 activation to an antiviral program Nat. Commun. 2019 10 1 14 10.1038/s41467-019-12894-z 31653857 PMC6814756 · DOI
  192. [207]Yun S.-M. Kim Y.S. Hur D.Y. LMP1 and 2A Induce the Expression of Nrf2 Through Akt Signaling Pathway in Epstein-Barr Virus–Transformed B Cells Transl. Oncol. 2019 12 775 783 10.1016/j.tranon.2019.02.009 30909091 PMC6434054 · DOI
  193. [208]Feng J. Chen Q. Zhang P. Huang X. Xie W. Zhang H. Yao P. Latent Membrane Protein 1 Promotes Tumorigenesis Through Upregulation of PGC1beta Signaling Pathway Stem Cell Rev. Rep. 2021 17 1486 1499 10.1007/s12015-020-10112-8 33423158 PMC8316210 · DOI
  194. [209]Wang W. Zhang Y. Liu W. Zhang X. Xiao H. Zhao M. Luo B. CXCR4 induces cell autophagy and maintains EBV latent infection in EBVaGC Theranostics 2020 10 11549 11561 10.7150/thno.44251 33052232 PMC7545993 · DOI
  195. [210]Olagnier D. Farahani E. Thyrsted J. Blay-Cadanet J. Herengt A. Idorn M. Hait A. Hernaez B. Knudsen A. Iversen M.B. SARS-CoV2-mediated suppression of NRF2-signaling reveals potent antiviral and anti-inflammatory activity of 4-octyl-itaconate and dimethyl fumarate Nat. Commun. 2020 11 4938 10.1038/s41467-020-18764-3 33009401 PMC7532469 · DOI
  196. [211]Takiuchi Y. Kobayashi M. Tada K. Iwai F. Sakurada M. Hirabayashi S. Nagata K. Shirakawa K. Shindo K. Yasunaga J.-I. HTLV-1 bZIP factor suppresses TDP1 expression through inhibition of NRF-1 in adult T-cell leukemia Sci. Rep. 2017 7 12849 10.1038/s41598-017-12924-0 28993637 PMC5634466 · DOI
  197. [212]Suliman H.B. Kraft B. Bartz R. Chen L. Welty-Wolf K.E. Piantadosi C.A. Mitochondrial quality control in alveolar epithelial cells damaged by S. aureus pneumonia in mice Am. J. Physiol. Cell. Mol. Physiol. 2017 313 L699 L709 10.1152/ajplung.00197.2017 28663335 PMC6148085 · DOI
  198. [213]Bartz R.R. Suliman H.B. Fu P. Welty-Wolf K. Carraway M.S. MacGarvey N.C. Withers C.M. Sweeney T.E. Piantadosi C.A. Staphylococcus aureus sepsis and mito-chondrial accrual of the 8-oxoguanine DNA glycosylase DNA repair enzyme in mice Am. J. Respir. Crit. Care Med. 2011 183 226 233 10.1164/rccm.200911-1709OC 20732986 PMC3040391 · DOI
  199. [214]Bartz R.R. Fu P. Suliman H.B. Crowley S.D. MacGarvey N.C. Welty-Wolf K. Piantadosi C.A. Staphylococcus aureus Sepsis Induces Early Renal Mitochondrial DNA Repair and Mitochondrial Biogenesis in Mice PLoS ONE 2014 9 e100912 10.1371/journal.pone.0100912 24988481 PMC4079589 · DOI
  200. [215]Suliman H.B. Babiker A. Withers C.M. Sweeney T.E. Carraway M.S. Tatro L.G. Bartz R.R. Welty-Wolf K.E. Piantadosi C.A. Nitric oxide synthase-2 regulates mito-chondrial Hsp60 chaperone function during bacterial peritonitis in mice Free Radic. Biol. Med. 2010 48 736 746 10.1016/j.freeradbiomed.2009.12.019 20043987 PMC2842938 · DOI

200 of 244 shown

Authors
Andrieux, P., Chevillard, C., Cunha-Neto, E., & Nunes, J. P. S.
Affiliations
  • Inserm (FR)
  • Laboratory of Immunology, Heart Institute (InCor), Division of Clinical Immunology and Allergy, School of Medicine, University of São Paulo, São Paulo 05403-000, Brazil
Corresponding author
  • Chevillard, Christophe
  • Nunes, João Paulo Silva
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2021-10-20
Volume
22
Issue
21
Pages
11338
ISSN
1422-0067 (ISSN-L)
OpenAlex
W3207310604
Cited by
346
References
266
Citations by year
2026: 56 · 2025: 115 · 2024: 91 · 2023: 62 · 2022: 22
FWCI
4.59
Type
journal article
Language
en
Open access
Locations
  • International Journal of Molecular Sciences (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, other-oa)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • HAL AMU (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • the Institut National de la Santé et de la Recherche Médicale (INSERM) (none)
  • the Aix-Marseille University (AMIDEX “International_2018” MITOMUTCHAGAS)
  • the French Agency for Research (Agence Nationale de la Recherche-ANR) (Br-Fr-Chagas, landscardio)
  • the CNPq (Brazilian Council for Scientific and Technological Development) (none)
  • the FAPESP (São Paulo State Research Funding Agency Brazil) (2013/50302-3, 2014/50890-5)
  • the National Institutes of Health/USA (2 P50 AI098461-02, 2U19AI098461-06)
  • the Inserm Cross-Cutting Project GOLD (none)
  • the Excellence Initiative of Aix-Marseille University - A*Midex (Institute MarMaRa AMX-19-IET-007)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords
mitochondria, infection, inflammation, reactive oxygen species, oxidative phosphorylation, mitochondrial network, mitochondrial-nuclear communication, pathogen evasion, endosymbiotic origin of mitochondria, chronic inflammatory diseases, infectious diseases
MeSH terms
Animals, Energy Metabolism, Humans, Infections, Inflammation, Mitochondria, Mitochondrial Dynamics

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review