The SARS-CoV2 and mitochondria: the impact on cell fate
SARS-CoV2 and mitochondria
Keywords:
Coronavirus; endoplasmic reticulum stress; mitochondria; apoptosis; autophagy; mitochondrial fusion; immune system.Abstract
Coronavirus infection causes endoplasmic reticulum stress inside the cells, which inhibits protein folding. Prolonged endoplasmic reticulum stress causes an apoptotic process of unfolded protein response-induced cell death. Endoplasmic reticulum stress rapidly induces the activation of mTORC1, responsible for the induction of the IRE1-JNK pathway. IRE1-JNK stands out for its dual nature: pro-apoptotic in the first stage of infection, anti-apoptotic in persistently infected cells. Once penetrated the cells, the virus can deflect the mitochondrial function by implementing both waterfalls pro-apoptotic and anti-apoptotic response. The virus prevents, through Open Reading Frame 9b (ORF-9b) interacting with mitochondria, the response of the type I interferon of the cells affected by the infection and is fundamental for generating an antiviral cellular state. ORF-9b has effects on mitochondrial dynamics, inducing fusion and autophagy and promoting cell survival. The recognition of ORF-9b has made it possible to identify it as a molecular target of some existing potentially effective drugs (Midostaurin and Ruxolitinib). Other drugs, with the same target, are currently being tested. Given the great importance of mitochondria in virus-host interaction, in-depth knowledge of the actors and pathways involved is essential to continue developing new therapeutic strategies against SARS CoV2.
References
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23. Oostra M, te Lintelo EG, Deijs M, Verheije MH, Rottier PJM, de Haan CAM. Localization and Membrane Topology of Coronavirus Nonstructural Protein 4: Involvement of the Early Secretory Pathway in Replication. J Virol. 2007 Nov 15;81(22):12323–36.
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25. Snijder EJ, van der Meer Y, Zevenhoven-Dobbe J, Onderwater JJM, van der Meulen J, Koerten HK, et al. Ultrastructure and Origin of Membrane Vesicles Associated with the Severe Acute Respiratory Syndrome Coronavirus Replication Complex. J Virol. 2006 Jun 15;80(12):5927–40.
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29. Fung TS, Liu DX. Coronavirus infection, ER stress, apoptosis and innate immunity. Vol. 5, Frontiers in Microbiology. Frontiers Research Foundation; 2014.
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31. Reshi L, Wang H-V, Hong J-R. Modulation of Mitochondria During Viral Infections. In: Mitochondrial Diseases. InTech; 2018.
32. Bardanzellu F, Pintus MC, Fanos V, Marcialis MA. Once we were bacteria.. mitochondria to infinity and beyond. Vol. 8, Journal of Pediatric and Neonatal Individualized Medicine. Hygeia Press di Corridori Marinella; 2019. p. e080106.
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34. Wallace DC. A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine. Annu Rev Genet. 2005 Dec;39(1):359–407.
35. Reshi ML, Su Y-C, Hong J-R. RNA Viruses: ROS-Mediated Cell Death. Int J Cell Biol. 2014;2014.
36. Glingston RS, Deb R, Kumar S, Nagotu S. Organelle dynamics and viral infections: at cross roads. Vol. 21, Microbes and Infection. Elsevier Masson SAS; 2019. p. 20–32.
37. Woodward CL, Prakobwanakit S, Mosessian S, Chow SA. Integrase Interacts with Nucleoporin NUP153 To Mediate the Nuclear Import of Human Immunodeficiency Virus Type 1. J Virol. 2009 Jul 1;83(13):6522–33.
38. Khan M, Syed GH, Kim SJ, Siddiqui A. Mitochondrial dynamics and viral infections: A close nexus. Vol. 1853, Biochimica et Biophysica Acta - Molecular Cell Research. Elsevier; 2015. p. 2822–33.
39. Chan DC. Mitochondria: Dynamic Organelles in Disease, Aging, and Development. Vol. 125, Cell. Elsevier; 2006. p. 1241–52.
40. Chen H, Chan DC. Mitochondrial dynamics--fusion, fission, movement, and mitophagy--in neurodegenerative diseases. Hum Mol Genet [Internet]. 2009 Oct 15;18(R2):R169–76. Available from: https://pubmed.ncbi.nlm.nih.gov/19808793
41. [Recognition of Pathogens by Innate Immunity] - PubMed [Internet]. [cited 2020 May 17]. Available from: https://pubmed.ncbi.nlm.nih.gov/19188883/
42. Mitochondria: More than Just “Power Plants” in Stem Cells [Internet]. [cited 2020 May 17]. Available from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5660791/
43. Castanier C, Garcin D, Vazquez A, Arnoult D. Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway. EMBO Rep. 2010 Feb;11(2):133–8.
44. Fukushi M, Yoshinaka Y, Matsuoka Y, Hatakeyama S, Ishizaka Y, Kirikae T, et al. Monitoring of S Protein Maturation in the Endoplasmic Reticulum by Calnexin Is Important for the Infectivity of Severe Acute Respiratory Syndrome Coronavirus. J Virol. 2012 Nov 1;86(21):11745–53.
45. Taylor RC, Cullen SP, Martin SJ. Apoptosis: Controlled demolition at the cellular level. Vol. 9, Nature Reviews Molecular Cell Biology. Nature Publishing Group; 2008. p. 231–41.
46. Ogata M, Hino S -i., Saito A, Morikawa K, Kondo S, Kanemoto S, et al. Autophagy Is Activated for Cell Survival after Endoplasmic Reticulum Stress. Mol Cell Biol. 2006 Dec 15;26(24):9220–31.
47. Urano F, Wang XZ, Bertolotti A, Zhang Y, Chung P, Harding HP, et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science (80- ). 2000 Jan 28;287(5453):664–6.
48. Smeal T, Binetruy B, Mercola DA, Birrer M, Karin M. Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73. Nature. 1991;354(6353):494–6.
49. Yamamoto K, Ichijo H, Korsmeyer SJ. BCL-2 Is Phosphorylated and Inactivated by an ASK1/Jun N-Terminal Protein Kinase Pathway Normally Activated at G 2 /M . Mol Cell Biol. 1999 Dec 1;19(12):8469–78.
50. Mizutani T, Fukushi S, Saijo M, Kurane I, Morikawa S. JNK and PI3k/Akt signaling pathways are required for establishing persistent SARS-CoV infection in Vero E6 cells. Biochim Biophys Acta - Mol Basis Dis. 2005 Jun 30;1741(1–2):4–10.
51. Spiegel M, Pichlmair A, Martinez-Sobrido L, Cros J, Garcia-Sastre A, Haller O, et al. Inhibition of Beta Interferon Induction by Severe Acute Respiratory Syndrome Coronavirus Suggests a Two-Step Model for Activation of Interferon Regulatory Factor 3. J Virol. 2005 Feb 15;79(4):2079–86.
52. Shi C-S, Qi H-Y, Boularan C, Huang N-N, Abu-Asab M, Shelhamer JH, et al. SARS-Coronavirus Open Reading Frame-9b Suppresses Innate Immunity by Targeting Mitochondria and the MAVS/TRAF3/TRAF6 Signalosome. J Immunol. 2014 Sep 15;193(6):3080–9.
53. Kawai T, Akira S. Antiviral Signaling Through Pattern Recognition Receptors. J Biochem [Internet]. 2006 Dec 26;141(2):137–45. Available from: https://doi.org/10.1093/jb/mvm032
54. You F, Sun H, Zhou X, Sun W, Liang S, Zhai Z, et al. PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4. Nat Immunol. 2009 Nov 1;10(12):1300–8.
55. Maier HJ, Britton P. Involvement of autophagy in coronavirus replication. Vol. 4, Viruses. Multidisciplinary Digital Publishing Institute (MDPI); 2012. p. 3440–51.
56. Youle RJ, Van Der Bliek AM. Mitochondrial fission, fusion, and stress. Vol. 337, Science. American Association for the Advancement of Science; 2012. p. 1062–5.
57. Rambold AS, Kostelecky B, Elia N, Lippincott-Schwartz J. Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation. Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10190–5.
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11-05-2022
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Copyright (c) 2022 Eleonora Madeddu, Barbara Maniga, Marco Zaffanello, Vassilios Fanos, Antonietta Marcialis
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Madeddu E, Maniga B, Zaffanello M, Fanos V, Marcialis A. The SARS-CoV2 and mitochondria: the impact on cell fate: SARS-CoV2 and mitochondria. Acta Biomed [Internet]. 2022 May 11 [cited 2024 Jul. 17];93(2):e2022199. Available from: https://mattioli1885journals.com/index.php/actabiomedica/article/view/10327
