1,019
Views
0
CrossRef citations to date
0
Altmetric
EV71-a major emerging threat to children in Asia

Tribbles pseudokinase 3 promotes enterovirus A71 infection via dual mechanisms

, , , , , , , & show all
Article: 2307514 | Received 07 Dec 2023, Accepted 16 Jan 2024, Published online: 30 Jan 2024

References

  • Wang H, Li Y. Recent progress on functional genomics research of enterovirus 71. Virol Sin. 2019;34(1):9–21. doi:10.1007/s12250-018-0071-9
  • McMinn PC. Recent advances in the molecular epidemiology and control of human enterovirus 71 infection. Curr Opin Virol. 2012;2(2):199–205. doi:10.1016/j.coviro.2012.02.009
  • Wang SM, Liu CC. Enterovirus 71: epidemiology, pathogenesis and management. Expert Rev Anti Infect Ther. 2009;7(6):735–742. doi:10.1586/eri.09.45
  • Weng KF, Chen LL, Huang PN, et al. Neural pathogenesis of enterovirus 71 infection. Microbes Infect. 2010;12(7):505–510. doi:10.1016/j.micinf.2010.03.006
  • Wang SM, Lei HY, Liu CC. Cytokine immunopathogenesis of enterovirus 71 brain stem encephalitis. Clin Dev Immunol. 2012;2012:876241.
  • Xu Y, Zheng Y, Shi W, et al. Pathogenic characteristics of hand, foot and mouth disease in Shaanxi Province, China, 2010–2016. Sci Rep. 2020;10(1):989. doi:10.1038/s41598-020-57807-z
  • Schmidt NJ, Lennette EH, Ho HH. An apparently new enterovirus isolated from patients with disease of the central nervous system. J Infect Dis. 1974;129(3):304–309. doi:10.1093/infdis/129.3.304
  • Yamayoshi S, Yamashita Y, Li J, et al. Scavenger receptor B2 is a cellular receptor for enterovirus 71. Nat Med. 2009;15(7):798–801. doi:10.1038/nm.1992
  • Kobayashi K, Koike S. Cellular receptors for enterovirus A71. J Biomed Sci. 2020;27(1):23. doi:10.1186/s12929-020-0615-9
  • Dang M, Wang X, Wang Q, et al. Molecular mechanism of SCARB2-mediated attachment and uncoating of EV71. Protein Cell. 2014;5(9):692–703. doi:10.1007/s13238-014-0087-3
  • Bedard KM, Semler BL. Regulation of picornavirus gene expression. Microbes Infect. 2004;6(7):702–713. doi:10.1016/j.micinf.2004.03.001
  • Solomon T, Lewthwaite P, Perera D, et al. Virology, epidemiology, pathogenesis, and control of enterovirus 71. Lancet Infect Dis. 2010;10(11):778–790. doi:10.1016/S1473-3099(10)70194-8
  • He QQ, Ren S, Xia ZC, et al. Fibronectin facilitates enterovirus 71 infection by mediating viral entry. J Virol. 2018;92(9):e02251-17.
  • Huang PN, Lin JY, Locker N, et al. Far upstream element binding protein 1 binds the internal ribosomal entry site of enterovirus 71 and enhances viral translation and viral growth. Nucleic Acids Res. 2011;39(22):9633–9648. doi:10.1093/nar/gkr682
  • Lin JY, Li ML, Huang PN, et al. Heterogeneous nuclear ribonuclear protein K interacts with the enterovirus 71 5′ untranslated region and participates in virus replication. J Gen Virol. 2008;89(Pt 10):2540–2549. doi:10.1099/vir.0.2008/003673-0
  • Lin JY, Li ML, Shih SR. Far upstream element binding protein 2 interacts with enterovirus 71 internal ribosomal entry site and negatively regulates viral translation. Nucleic Acids Res. 2009;37(1):47–59. doi:10.1093/nar/gkn901
  • Lin JY, Shih SR, Pan M, et al. hnRNP A1 interacts with the 5’ untranslated regions of enterovirus 71 and Sindbis virus RNA and is required for viral replication. J Virol. 2009;83(12):6106–6114. doi:10.1128/JVI.02476-08
  • Zhao X, Yuan H, Yang H, et al. N-Acetyltransferase 8 promotes viral replication by increasing the stability of enterovirus 71 nonstructural proteins. J Virol. 2022;96(6):e0011922. doi:10.1128/jvi.00119-22
  • Su YS, Hsieh PY, Li JS, et al. The heat shock protein 70 family of chaperones regulates all phases of the enterovirus A71 life cycle. Front Microbiol. 2020;11:1656. doi:10.3389/fmicb.2020.01656
  • Wang RY, Kuo RL, Ma WC, et al. Heat shock protein-90-beta facilitates enterovirus 71 viral particles assembly. Virology. 2013;443(2):236–247. doi:10.1016/j.virol.2013.05.001
  • Salazar M, Lorente M, Orea-Soufi A, et al. Oncosuppressive functions of tribbles pseudokinase 3. Biochem Soc Trans. 2015;43(5):1122–1126. doi:10.1042/BST20150124
  • Kiss-Toth E, Bagstaff SM, Sung HY, et al. Human tribbles, a protein family controlling mitogen-activated protein kinase cascades. J Biol Chem. 2004;279(41):42703–8. doi:10.1074/jbc.M407732200
  • Yokoyama T, Nakamura T. Tribbles in disease: signaling pathways important for cellular function and neoplastic transformation. Cancer Sci. 2011;102(6):1115–1122. doi:10.1111/j.1349-7006.2011.01914.x
  • Lohan F, Keeshan K. The functionally diverse roles of tribbles. Biochem Soc Trans. 2013;41(4):1096–1100. doi:10.1042/BST20130105
  • Masoner V, Das R, Pence L, et al. The kinase domain of Drosophila Tribbles is required for turnover of fly C/EBP during cellmigration. Dev Biol. 2013;375(1):33–44. doi:10.1016/j.ydbio.2012.12.016
  • Hua F, Mu R, Liu J, et al. TRB3 interacts with SMAD3 promoting tumor cell migration and invasion. J Cell Sci. 2011;124(Pt 19):3235–3246. doi:10.1242/jcs.082875
  • Ohoka N, Yoshii S, Hattori T, et al. TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. EMBO J. 2005;24(6):1243–1255. doi:10.1038/sj.emboj.7600596
  • Zhang W, Yang Z, Li X, et al. The functional Q84R polymorphism of TRIB3 gene is associated with diabetic nephropathy in Chinese type 2 diabetic patients. Gene. 2015;555(2):357–361. doi:10.1016/j.gene.2014.11.031
  • Schwarzer R, Dames S, Tondera D, et al. TRB3 is a PI 3-kinase dependent indicator for nutrient starvation. Cell Signal. 2006;18(6):899–909. doi:10.1016/j.cellsig.2005.08.002
  • Shen P, Zhang TY, Wang SY. TRIB3 promotes oral squamous cell carcinoma cell proliferation by activating the AKT signaling pathway. Exp Ther Med. 2021;21(4):313. doi:10.3892/etm.2021.9744
  • Ord D, Ord T. Characterization of human NIPK (TRB3, SKIP3) gene activation in stressful conditions. Biochem Biophys Res Commun. 2005;330(1):210–218. doi:10.1016/j.bbrc.2005.02.149
  • Mondal D, Mathur A, Chandra PK. Tripping on TRIB3 at the junction of health, metabolic dysfunction and cancer. Biochimie. 2016;124:34–52. doi:10.1016/j.biochi.2016.02.005
  • Wennemers M, Bussink J, Scheijen B, et al. Tribbles homolog 3 denotes a poor prognosis in breast cancer and is involved in hypoxia response. Breast Cancer Res. 2011;13(4):R82. doi:10.1186/bcr2934
  • Prudente S, Sesti G, Pandolfi A, et al. The mammalian tribbles homolog TRIB3, glucose homeostasis, and cardiovascular diseases. Endocr Rev. 2012;33(4):526–546. doi:10.1210/er.2011-1042
  • Shang S, Yang YW, Chen F, et al. TRIB3 reduces CD8+ T cell infiltration and induces immune evasion by repressing the STAT1-CXCL10 axis in colorectal cancer. Sci Transl Med. 2022;14(626):eabf0992. doi:10.1126/scitranslmed.abf0992
  • Li K, Wang F, Cao WB, et al. Trib3 promotes APL progression through stabilization of the oncoprotein PML-RARα and inhibition of p53-mediated senescence. Cancer Cell. 2017;31(5):697–710.e7. doi:10.1016/j.ccell.2017.04.006
  • Lv X, Liu S, Liu C, et al. TRIB3 promotes pulmonary fibrosis through inhibiting SLUG degradation by physically interacting with MDM2. Acta Pharm Sin B. 2023;13(4):1631–1647. doi:10.1016/j.apsb.2023.01.008
  • Chen QZ, Chen Y, Li X, et al. Trib3 interacts with STAT3 to promote cancer angiogenesis. Curr Med Sci. 2022;42(5):932–940. doi:10.1007/s11596-022-2655-8
  • Tran SC, Pham TM, Nguyen LN, et al. Nonstructural 3 protein of hepatitis C virus modulates the tribbles homolog 3/Akt signaling pathway for persistent viral infection. J Virol. 2016;90(16):7231–7247. doi:10.1128/JVI.00326-16
  • Yamane D, Zahoor MA, Mohamed YM, et al. Microarray analysis reveals distinct signaling pathways transcriptionally activated by infection with bovine viral diarrhea virus in different cell types. Virus Res. 2009;142(1–2):188–199. doi:10.1016/j.virusres.2009.02.015
  • Carr M, Gonzalez G, Martinelli A, et al. Upregulated expression of the antioxidant sestrin 2 identified by transcriptomic analysis of Japanese encephalitis virus-infected SH-SY5Y neuroblastoma cells. Virus Genes. 2019;55(5):630–642. doi:10.1007/s11262-019-01683-x
  • Cury SS, Oliveira JS, Biagi-Júnior CAO, et al. Transcriptional profiles and common genes link lung cancer with the development and severity of COVID-19. Gene. 2023;852:147047. doi:10.1016/j.gene.2022.147047
  • de Moraes D, Paiva BVB, Cury SS, et al. Prediction of SARS-CoV interaction with host proteins during lung aging reveals a potential role for TRIB3 in COVID-19. Aging Dis. 2021;12(1):42–49. doi:10.14336/AD.2020.1112
  • Hua F, Li K, Yu JJ, et al. TRB3 links insulin/IGF to tumour promotion by interacting with p62 and impeding autophagic/proteasomal degradations. Nat Commun. 2015;6:7951. doi:10.1038/ncomms8951
  • Wang F, Gao Y, Xue S, et al. SCARB2 drives hepatocellular carcinoma tumor initiating cells via enhanced MYC transcriptional activity. Nat Commun. 2023;14(1):5917. doi:10.1038/s41467-023-41593-z
  • Liu J, Yang Y, Xu Y, et al. Lycorine reduces mortality of human enterovirus 71-infected mice by inhibiting virus replication. Virol J. 2011;8:483. doi:10.1186/1743-422X-8-483
  • Wang H, Cui B, Yan H, et al. Targeting 7-dehydrocholesterol reductase against EV-A71 replication by upregulating interferon response. Antiviral Res. 2023;209:105497. doi:10.1016/j.antiviral.2022.105497
  • Hua F, Shang S, Yang YW, et al. Trib3 interacts with β-catenin and TCF4 to increase stem cell features of colorectal cancer stem cells and tumorigenesis. Gastroenterology. 2019;156(3):708–721.e15. doi:10.1053/j.gastro.2018.10.031
  • Wang H, Zhong M, Cui B, et al. Neddylation of enterovirus 71 VP2 protein reduces its stability and restricts viral replication. J Virol. 2022;96(10):e0059822. doi:10.1128/jvi.00598-22
  • Li K, Wang F, Yang ZN, et al. TRIB3 promotes MYC-associated lymphoma development through suppression of UBE3B-mediated MYC degradation. Nat Commun. 2020;11(1):6316. doi:10.1038/s41467-020-20107-1
  • Zhu YP, Peng ZG, Wu ZY, et al. Host APOBEC3G protein inhibits HCV replication through direct binding at NS3. PLoS One. 2015;10(3):e0121608.
  • Zhao D, Wang X, Lou G, et al. APOBEC3G directly binds Hepatitis B virus core protein in cell and cell free systems. Virus Res. 2010;151(2):213–219. doi:10.1016/j.virusres.2010.05.009
  • Lin YW, Lin HY, Tsou YL, et al. Human SCARB2-mediated entry and endocytosis of EV71. PLoS One. 2012;7(1):e30507. doi:10.1371/journal.pone.0030507
  • Richmond L, Keeshan K. Pseudokinases: a tribble-edged sword. FEBS J. 2020;287(19):4170–4182. doi:10.1111/febs.15096
  • Tracz M, Bialek W. Beyond K48 and K63: non-canonical protein ubiquitination. Cell Mol Biol Lett. 2021;26(1):1. doi:10.1186/s11658-020-00245-6
  • Wang HQ, Jiang JD, Li YH. Acta Pharm Sin. 2013;48:343–346.
  • Shang YY, Zhong M, Zhang LP, et al. Tribble 3, a novel oxidized low-density lipoprotein-inducible gene, is induced via the activating transcription factor 4–C/EBP homologous protein pathway. Clin Exp Pharmacol Physiol. 2010;37(1):51–55. doi:10.1111/j.1440-1681.2009.05229.x
  • Steverson D, Jr., Tian L, Fu Y, et al. Tribbles homolog 3 promotes foam cell formation associated with decreased proinflammatory cytokine production in macrophages: evidence for reciprocal regulation of cholesterol uptake and inflammation. Metab Syndr Relat Disord. 2016;14(1):7–15. doi:10.1089/met.2015.0037
  • Borsting E, Patel SV, Declèves AE, et al. Tribbles homolog 3 attenuates mammalian target of rapamycin complex-2 signaling and inflammation in the diabetic kidney. J Am Soc Nephrol. 2014;25(9):2067–2078. doi:10.1681/ASN.2013070811