4,030
Views
32
CrossRef citations to date
0
Altmetric
Articles

Swine acute diarrhea syndrome coronavirus-induced apoptosis is caspase- and cyclophilin D- dependent

, , , , , , , , , , , , & show all
Pages 439-456 | Received 28 Sep 2019, Accepted 15 Jan 2020, Published online: 24 Feb 2020

References

  • Galluzzi L, Kepp O, Trojel-Hansen C, et al. Mitochondrial control of cellular life, stress, and death. Circ Res. 2012;111(9):1198–1207.
  • Kroemer G, Galluzzi L, Vandenabeele P, et al. Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009. Cell Death Differ. 2009;16(1):3–11.
  • Arch RH, Thompson CB. Lymphocyte survival–the struggle against death. Annu Rev Cell Dev Biol. 1999;15:113–140.
  • Shih WL, Hsu HW, Liao MH, et al. Avian reovirus sigmaC protein induces apoptosis in cultured cells. Virology. 2004;321(1):65–74.
  • Everett H, McFadden G. Apoptosis: an innate immune response to virus infection. Trends Microbiol. 1999;7(4):160–165.
  • Lee SM, Kleiboeker SB. Porcine reproductive and respiratory syndrome virus induces apoptosis through a mitochondria-mediated pathway. Virology. 2007;365(2):419–434.
  • Cryns V, Yuan J. Proteases to die for. Genes Dev. 1998;12(11):1551–1570.
  • O’Brien V. Viruses and apoptosis. J Gen Virol. 1998;79(Pt 8):1833–1845.
  • Razvi ES, Welsh RM. Apoptosis in viral infections. Adv Virus Res. 1995;45:1–60.
  • Ding L, Xu X, Huang Y, et al. Transmissible gastroenteritis virus infection induces apoptosis through FasL- and mitochondria-mediated pathways. Vet Microbiol. 2012;158(1–2):12–22.
  • Kim Y, Lee C. Porcine epidemic diarrhea virus induces caspase-independent apoptosis through activation of mitochondrial apoptosis-inducing factor. Virology. 2014;460–461:180–193.
  • Lee YJ, Lee C. Porcine deltacoronavirus induces caspase-dependent apoptosis through activation of the cytochrome c -mediated intrinsic mitochondrial pathway. Virus Res. 2018;253:112–123.
  • Ziebuhr J, Snijder EJ, Gorbalenya AE. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J Gen Virol. 2000;81(Pt 4):853–879.
  • Siddell S, Wege H, Ter Meulen V. The biology of coronaviruses. J Gen Virol. 1983;64(Pt 4):761–776.
  • Zhou P, Fan H, Lan T, et al. Fatal swine acute diarrhoea syndrome caused by an HKU2-related coronavirus of bat origin. Nature. 2018;556(7700):255–258.
  • Shi D, Shi H, Sun D, et al. Nucleocapsid Interacts with NPM1 and protects it from proteolytic cleavage, enhancing cell survival, and is involved in PEDV growth. Sci Rep. 2017;7:39700.
  • Han Y, Zhang J, Shi H, et al. Epitope mapping and cellular localization of swine acute diarrhea syndrome coronavirus nucleocapsid protein using a novel monoclonal antibody. Virus Res. 2019;197752.
  • Hierholzer JC, Killington RA. Virus isolation and quantitation. 1996.
  • Hinshaw VS, Olsen CW, Dybdahl-Sissoko N, et al. Apoptosis: a mechanism of cell killing by influenza A and B viruses. J Virol. 1994;68(6):3667–3673.
  • Xue M, Fu F, Ma Y, et al. The PERK Arm of the unfolded protein response negatively regulates transmissible gastroenteritis virus replication by suppressing protein translation and promoting type I interferon production. J Virol. 2018;92(15):e00431–18.
  • Thornberry NA, Lazebnik Y. Caspases: enemies within. Science. 1998;281(5381):1312–1316.
  • Nicholson DW, Thornberry NA. Caspases: killer proteases. Trends Biochem Sci. 1997;22(8):299–306.
  • Henkart PA. ICE family proteases: mediators of all apoptotic cell death? Immunity. 1996;4(3):195–201.
  • Dubrez L, Savoy I, Hamman A, et al. Pivotal role of a DEVD-sensitive step in etoposide-induced and Fas-mediated apoptotic pathways. EMBO J. 1996;15(20):5504–5512.
  • Enari M, Hug H, Nagata S. Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature. 1995;375(6526):78–81.
  • Jacobsen MD, Weil M, Raff MC. Role of Ced-3/ICE-family proteases in staurosporine-induced programmed cell death. J Cell Biol. 1996;133(5):1041–1051.
  • Muzio M, Chinnaiyan AM, Kischkel FC, et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death–inducing signaling complex. Cell. 1996;85(6):817–827.
  • Clarke P, Tyler KL. Apoptosis in animal models of virus-induced disease. Nat Rev Microbiol. 2009;7(2):144–155.
  • Roy S, Nicholson DW. Cross-talk in cell death signaling. J Exp Med. 2000;192(8):F21–F25.
  • Yin XM. Signal transduction mediated by Bid, a pro-death Bcl-2 family proteins, connects the death receptor and mitochondria apoptosis pathways. Cell Res. 2000;10(3):161–167.
  • Halestrap AP, McStay GP, Clarke SJ. The permeability transition pore complex: another view. Biochimie. 2002;84(2–3):153–166.
  • Wei MC, Zong WX, Cheng EH, et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science. 2001;292(5517):727–730.
  • Suh DH, Kim MK, Kim HS, et al. Mitochondrial permeability transition pore as a selective target for anti-cancer therapy. Front Oncol. 2013;3:41.
  • Baines CP, Kaiser RA, Purcell NH, et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature. 2005;434(7033):658–662.
  • Eleouet JF, Chilmonczyk S, Besnardeau L, et al. Transmissible gastroenteritis coronavirus induces programmed cell death in infected cells through a caspase-dependent pathway. J Virol. 1998;72(6):4918–4924.
  • Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001;75(14):6402–6409.
  • Liu Y, Cai Y, Zhang X. Induction of caspase-dependent apoptosis in cultured rat oligodendrocytes by murine coronavirus is mediated during cell entry and does not require virus replication. J Virol. 2003;77(22):11952–11963.
  • Chen CJ, Makino S. Murine coronavirus-induced apoptosis in 17Cl-1 cells involves a mitochondria-mediated pathway and its downstream caspase-8 activation and bid cleavage. Virology. 2002;302(2):321–332.
  • De Martino L, Marfe G, Longo M, et al. Bid cleavage, cytochrome c release and caspase activation in canine coronavirus-induced apoptosis. Vet Microbiol. 2010;141(1–2):36–45.
  • Deszcz L, Gaudernak E, Kuechler E, et al. Apoptotic events induced by human rhinovirus infection. J Gen Virol. 2005;86(Pt 5):1379–1389.
  • Gadaleta P, Perfetti X, Mersich S, et al. Early activation of the mitochondrial apoptotic pathway in Vesicular Stomatitis virus-infected cells. Virus Res. 2005;109(1):65–69.
  • Poole BD, Karetnyi YV, Naides SJ. Parvovirus B19-induced apoptosis of hepatocytes. J Virol. 2004;78(14):7775–7783.
  • Bartz SR, Emerman M. Human immunodeficiency virus type 1 Tat induces apoptosis and increases sensitivity to apoptotic signals by up-regulating FLICE/caspase-8. J Virol. 1999;73(3):1956–1963.
  • Bitzer M, Prinz F, Bauer M, et al. Sendai virus infection induces apoptosis through activation of caspase-8 (FLICE) and caspase-3 (CPP32). J Virol. 1999;73(1):702–708.
  • Kassis R, Larrous F, Estaquier J, et al. Lyssavirus matrix protein induces apoptosis by a TRAIL-dependent mechanism involving caspase-8 activation. J Virol. 2004;78(12):6543–6555.
  • Li XD, Kukkonen S, Vapalahti O, et al. Tula hantavirus infection of Vero E6 cells induces apoptosis involving caspase 8 activation. J Gen Virol. 2004 Nov;85(Pt 11):3261–3268.
  • Zhirnov OP, Ksenofontov AL, Kuzmina SG, et al. Interaction of influenza A virus M1 matrix protein with caspases. Biochemistry (Moscow). 2002;67(5):534–539.
  • Tepper CG, Seldin MF. Modulation of caspase-8 and FLICE-inhibitory protein expression as a potential mechanism of Epstein-Barr virus tumorigenesis in Burkitt’s lymphoma. Blood. 1999;94(5):1727–1737.
  • Connolly PF, Fearnhead HO. Viral hijacking of host caspases: an emerging category of pathogen-host interactions. Cell Death Differ. 2017;24(8):1401–1410.
  • Liu Y, Zhang X. Murine coronavirus-induced oligodendrocyte apoptosis is mediated through the activation of the Fas signaling pathway. Virology. 2007;360(2):364–375.
  • Lin CH, Shih WL, Lin FL, et al. Bovine ephemeral fever virus-induced apoptosis requires virus gene expression and activation of Fas and mitochondrial signaling pathway. Apoptosis. 2009;14(7):864–877.
  • Chou AH, Tsai HF, Wu YY, et al. Hepatitis C virus core protein modulates TRAIL-mediated apoptosis by enhancing Bid cleavage and activation of mitochondria apoptosis signaling pathway. J Immunol. 2005;174(4):2160–2166.
  • St-Louis MC, Massie B, Archambault D. The bovine viral diarrhea virus (BVDV) NS3 protein, when expressed alone in mammalian cells, induces apoptosis which correlates with caspase-8 and caspase-9 activation. Vet Res. 2005;36(2):213–227.
  • Otera H, Mihara K. Mitochondrial dynamics: functional link with apoptosis. Int J Cell Biol. 2012;2012:1–10.
  • Joza N, Susin SA, Daugas E, et al. Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. Nature. 2001;410(6828):549–554.
  • Ferri KF, Jacotot E, Blanco J, et al. Apoptosis control in syncytia induced by the HIV type 1-envelope glycoprotein complex: role of mitochondria and caspases. J Exp Med. 2000;192(8):1081–1092.
  • Zhou G, Roizman B. Wild-type herpes simplex virus 1 blocks programmed cell death and release of cytochrome c but not the translocation of mitochondrial apoptosis-inducing factor to the nuclei of human embryonic lung fibroblasts. J Virol. 2000;74(19):9048–9053.
  • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev. 2001;15(22):2922–2933.
  • Madesh M, Antonsson B, Srinivasula SM, et al. Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization. J Biol Chem. 2002;277(7):5651–5659.
  • Youle RJ, Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol. 2008;9(1):47–59.
  • Chipuk JE, Green DR. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol. 2008;18(4):157–164.
  • Deng L, Adachi T, Kitayama K, et al. Hepatitis C virus infection induces apoptosis through a Bax-triggered, mitochondrion-mediated, caspase 3-dependent pathway. J Virol. 2008;82(21):10375–10385.
  • Pearce AF, Lyles DS. Vesicular stomatitis virus induces apoptosis primarily through Bak rather than Bax by inactivating Mcl-1 and Bcl-XL. J Virol. 2009;83(18):9102–9112.
  • Parquet MC, Kumatori A, Hasebe F, et al. West Nile virus-induced bax-dependent apoptosis. FEBS Lett. 2001;500(1–2):17–24.
  • Green DR, Reed JC. Mitochondria and apoptosis. Science. 1998;281(5381):1309–1312.
  • de Wilde AH, Li Y, van der Meer Y, et al. Cyclophilin inhibitors block arterivirus replication by interfering with viral RNA synthesis. J Virol. 2013;87(3):1454–1464.
  • Kambara H, Tani H, Mori Y, et al. Involvement of cyclophilin B in the replication of Japanese encephalitis virus. Virology. 2011;412(1):211–219.
  • Nakagawa M, Sakamoto N, Enomoto N, et al. Specific inhibition of hepatitis C virus replication by cyclosporin A. Biochem Biophys Res Commun. 2004;313(1):42–47.
  • Pfefferle S, Schopf J, Kogl M, et al. The SARS-coronavirus-host interactome: identification of cyclophilins as target for pan-coronavirus inhibitors. PLoS Pathog. 2011;7(10):e1002331.
  • Qing M, Yang F, Zhang B, et al. Cyclosporine inhibits flavivirus replication through blocking the interaction between host cyclophilins and viral NS5 protein. Antimicrob Agents Chemother. 2009;53(8):3226–3235.