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p38 activation and viral infection

Published online by Cambridge University Press:  21 January 2022

Luyao Wang
Affiliation:
State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan430072, Hubei, China
Zhiqiang Xia
Affiliation:
State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan430072, Hubei, China
Wei Tang
Affiliation:
State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan430072, Hubei, China
Yu Sun
Affiliation:
School of Medicine, Wuhan University of Science and Technology, Wuhan430065, Hubei, China
Yingliang Wu
Affiliation:
State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan430072, Hubei, China
Hang Fai Kwok*
Affiliation:
Frontiers Science Center for Precision Oncology of MoE, University of Macau, Taipa, Macau, China Faculty of Health Sciences, Cancer Center, University of Macau, Avenida de Universidade, Taipa, Macau, China
Fang Sun*
Affiliation:
State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan430072, Hubei, China Department of Biochemistry and Molecular Biology, College of Basic Medicine, Hubei University of Medicine, Shiyan442000, Hubei, China
Zhijian Cao*
Affiliation:
State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan430072, Hubei, China
*
Author for correspondence: Hang Fai Kwok, E-mail: hfkwok@um.edu.mo; Fang Sun, E-mail: 2016202040055@whu.edu.cn; Zhijian Cao, E-mail: zjcao@whu.edu.cn
Author for correspondence: Hang Fai Kwok, E-mail: hfkwok@um.edu.mo; Fang Sun, E-mail: 2016202040055@whu.edu.cn; Zhijian Cao, E-mail: zjcao@whu.edu.cn
Author for correspondence: Hang Fai Kwok, E-mail: hfkwok@um.edu.mo; Fang Sun, E-mail: 2016202040055@whu.edu.cn; Zhijian Cao, E-mail: zjcao@whu.edu.cn

Abstract

Viruses completely rely on the energy and metabolic systems of host cells for life activities. Viral infections usually lead to cytopathic effects and host diseases. To date, there are still no specific clinical vaccines or drugs against most viral infections. Therefore, understanding the molecular and cellular mechanisms of viral infections is of great significance to prevent and treat viral diseases. A variety of viral infections are related to the p38 MAPK signalling pathway, and p38 is an important host factor in virus-infected cells. Here, we introduce the different signalling pathways of p38 activation and then summarise how different viruses induce p38 phosphorylation. Finally, we provide a general summary of the effect of p38 activation on virus replication. Our review provides integrated data on p38 activation and viral infections and describes the potential application of targeting p38 as an antiviral strategy.

Type
Review
Copyright
Copyright © The Author(s), 2022. Published by Cambridge University Press

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References

Minton, K (2018) Viral tropism for tuft cells. Nature Reviews Immunology 18, 360361.CrossRefGoogle ScholarPubMed
Sun, E, He, J and Zhuang, X (2013) Live cell imaging of viral entry. Current Opinion in Virology 3, 3443.CrossRefGoogle ScholarPubMed
Ibrahim, B et al. (2018) Bioinformatics meets virology: the European virus bioinformatics center's second annual meeting. Viruses 10, 256274.CrossRefGoogle ScholarPubMed
Nomaguchi, M and Adachi, A (2010) Virology as biosystematics: towards understanding the viral infection biology. Frontiers in Microbiology 1, 2.CrossRefGoogle ScholarPubMed
Wilder-Smith, A, Chiew, CJ and Lee, VJ (2020) Can we contain the COVID-19 outbreak with the same measures as for SARS? The Lancet. Infectious Diseases 20, e102e107.CrossRefGoogle ScholarPubMed
Li, H et al. (2020) Impact of corticosteroid therapy on outcomes of persons with SARS-CoV-2, SARS-CoV, or MERS-CoV infection: a systematic review and meta-analysis. Leukemia 34, 15031511.CrossRefGoogle ScholarPubMed
Adachi, A (2020) Grand challenge in human/animal virology: unseen, smallest replicative entities shape the whole globe. Frontiers in Microbiology 11, 431.CrossRefGoogle ScholarPubMed
Gonçalves, BC et al. (2021) Antiviral therapies: advances and perspectives. Fundamental & Clinical Pharmacology 35, 305320.CrossRefGoogle ScholarPubMed
Galdiero, S et al. (2011) Silver nanoparticles as potential antiviral agents. Molecules 16, 88948918.CrossRefGoogle ScholarPubMed
Ison, MG (2017) Antiviral treatments. Clinics in Chest Medicine 38, 139153.CrossRefGoogle ScholarPubMed
Read, SA et al. (2019) The role of zinc in antiviral immunity. Advances in Nutrition 10, 696710.CrossRefGoogle ScholarPubMed
Martinez-Limon, A et al. (2020) The p38 pathway: from biology to cancer therapy. International Journal of Molecular Sciences 21, 19131930.CrossRefGoogle ScholarPubMed
Corre, I, Paris, F and Huot, J (2017) The p38 pathway, a major pleiotropic cascade that transduces stress and metastatic signals in endothelial cells. Oncotarget 8, 5568455714.CrossRefGoogle Scholar
Cuadrado, A and Nebreda, AR (2010) Mechanisms and functions of p38 MAPK signalling. Biochemical Journal 429, 403417.CrossRefGoogle ScholarPubMed
Enslen, H, Raingeaud, J and Davis, RJ (1998) Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6. Journal of Biological Chemistry 273, 17411748.CrossRefGoogle ScholarPubMed
Salvador, JM et al. (2005) Alternative p38 activation pathway mediated by T cell receptor-proximal tyrosine kinases. Nature Immunology 6, 390395.CrossRefGoogle Scholar
Zhang, Z, Rong, L and Li, YP (2019) Flaviviridae viruses and oxidative stress: implications for viral pathogenesis. Oxidative Medicine and Cellular Longevity 2019, 1409582.Google ScholarPubMed
Zhao, LJ et al. (2006) Up-regulation of ERK and p38 MAPK signaling pathways by hepatitis C virus E2 envelope protein in human T lymphoma cell line. Journal of Leukocyte Biology 80, 424432.CrossRefGoogle ScholarPubMed
Song, X et al. (2016) HCV core protein binds to gC1qR to induce A20 expression and inhibit cytokine production through MAPKs and NF-κB signaling pathways. Oncotarget 7, 3379633808.CrossRefGoogle ScholarPubMed
Moorman, JP et al. (2005) Induction of p38-and gC1qR-dependent IL-8 expression in pulmonary fibroblasts by soluble hepatitis C core protein. Respiratory Research 6, 105.CrossRefGoogle ScholarPubMed
Serti, E et al. (2011) Modulation of IL-2 expression after uptake of hepatitis C virus non-enveloped capsid-like particles: the role of p38 kinase. Cellular and Molecular Life Sciences 68, 505522.CrossRefGoogle ScholarPubMed
Zhu, S et al. (2017) p38 MAPK plays a critical role in induction of a pro-inflammatory phenotype of retinal Müller cells following zika virus infection. Antiviral Research 145, 7081.CrossRefGoogle Scholar
Barbachano-Guerrero, A, Endy, TP and King, CA (2020) Dengue virus non-structural protein 1 activates the p38 MAPK pathway to decrease barrier integrity in primary human endothelial cells. Journal of General Virology 101, 484496.CrossRefGoogle ScholarPubMed
To, J and Torres, J (2019) Viroporins in the influenza virus. Cells 8, 654673.CrossRefGoogle ScholarPubMed
Chow, EJ, Doyle, JD and Uyeki, TM (2019) Influenza virus-related critical illness: prevention, diagnosis, treatment. Critical Care 23, 214.CrossRefGoogle Scholar
Meineke, R, Rimmelzwaan, GF and Elbahesh, H (2019) Influenza virus infections and cellular kinases. Viruses 11, 171187.CrossRefGoogle ScholarPubMed
Choi, MS et al. (2016) A novel p38 mitogen activated protein kinase (MAPK) specific inhibitor suppresses respiratory syncytial virus and influenza A virus replication by inhibiting virus-induced p38 MAPK activation. Biochemical and Biophysical Research Communications 477, 311316.CrossRefGoogle ScholarPubMed
Nencioni, L et al. (2009) Bcl-2 expression and p38 MAPK activity in cells infected with influenza A virus: impact on virally induced apoptosis and viral replication. Journal of Biological Chemistry 284, 1600416015.CrossRefGoogle ScholarPubMed
Börgeling, Y et al. (2014) Inhibition of p38 mitogen-activated protein kinase impairs influenza virus-induced primary and secondary host gene responses and protects mice from lethal H5N1 infection. Journal of Biological Chemistry 289, 1327.CrossRefGoogle ScholarPubMed
Marchant, D et al. (2010) Toll-like receptor 4-mediated activation of p38 mitogen-activated protein kinase is a determinant of respiratory virus entry and tropism. Journal of Virology 84, 1135911373.CrossRefGoogle ScholarPubMed
Wu, RF et al. (2010) Nox4-derived H2O2 mediates endoplasmic reticulum signaling through local ras activation. Molecular and Cellular Biology 30, 35533568.CrossRefGoogle ScholarPubMed
Jaulmes, A et al. (2009) Nox4 mediates the expression of plasminogen activator inhibitor-1 via p38 MAPK pathway in cultured human endothelial cells. Thrombosis Research 124, 439446.CrossRefGoogle ScholarPubMed
Totura, AL and Baric, RS (2012) SARS coronavirus pathogenesis: host innate immune responses and viral antagonism of interferon. Current Opinion in Virology 2, 264275.CrossRefGoogle ScholarPubMed
Padhan, K et al. (2008) Severe acute respiratory syndrome coronavirus 3a protein activates the mitochondrial death pathway through p38 MAP kinase activation. Journal of General Virology 89, 19601969.CrossRefGoogle ScholarPubMed
Grimes, JM and Grimes, KV (2020) p38 MAPK inhibition: a promising therapeutic approach for COVID-19. Journal of Molecular and Cellular Cardiology 144, 6365.CrossRefGoogle ScholarPubMed
Fanales-Belasio, E et al. (2010) HIV virology and pathogenetic mechanisms of infection: a brief overview. Annali Dell'istituto Superiore di Sanita 46, 514.Google ScholarPubMed
Eberle, J and Gürtler, L (2012) HIV types, groups, subtypes and recombinant forms: errors in replication, selection pressure and quasispecies. Intervirology 55, 7983.CrossRefGoogle ScholarPubMed
Furler, RL and Uittenbogaart, CH (2010) Signaling through the p38 and ERK pathways: a common link between HIV replication and the immune response. Immunologic Research 48, 99109.CrossRefGoogle ScholarPubMed
Yuan, Y et al. (2008) CXCR4 receptor antagonist blocks cardiac myocyte p38 MAP kinase phosphorylation by HIV gp120. Cardiovascular Toxicology 8, 173180.CrossRefGoogle ScholarPubMed
Selb, B and Weber, B (1994) A study of human reovirus IgG and IgA antibodies by ELISA and western blot. Journal of Virological Methods 47, 1525.CrossRefGoogle ScholarPubMed
Errington, F et al. (2008) Inflammatory tumour cell killing by oncolytic reovirus for the treatment of melanoma. Gene Therapy 15, 12571270.CrossRefGoogle ScholarPubMed
Offit, PA (2018) Challenges to developing a rotavirus vaccine. Viral Immunology 31, 104108.CrossRefGoogle ScholarPubMed
Bruijning-Verhagen, P and Groome, M (2017) Rotavirus vaccine: current use and future considerations. Pediatric Infectious Disease Journal 36, 676678.CrossRefGoogle ScholarPubMed
Ji, WT et al. (2009) AMP-activated protein kinase facilitates avian reovirus to induce mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 3/6 signalling that is beneficial for virus replication. Journal of General Virology 90, 30023009.CrossRefGoogle ScholarPubMed
Holloway, G and Coulson, BS (2006) Rotavirus activates JNK and p38 signaling pathways in intestinal cells, leading to AP-1-driven transcriptional responses and enhanced virus replication. Journal of Virology 80, 1062410633.CrossRefGoogle ScholarPubMed
Ge, Y et al. (2013) Rotavirus NSP4 triggers secretion of proinflammatory cytokines from macrophages via Toll-like receptor 2. Journal of Virology 87, 11160–7.CrossRefGoogle ScholarPubMed
Di Fiore, IJ, Holloway, G and Coulson, BS (2015) Innate immune responses to rotavirus infection in macrophages depend on MAVS but involve neither the NLRP3 inflammasome nor JNK and p38 signaling pathways. Virus Research 208, 8997.CrossRefGoogle ScholarPubMed
Weaver, SC and Lecuit, M (2015) Chikungunya virus and the global spread of a mosquito-borne disease. New England Journal of Medicine 372, 12311239.CrossRefGoogle ScholarPubMed
Khan, AH et al. (2002) Complete nucleotide sequence of chikungunya virus and evidence for an internal polyadenylation site. Journal of General Virology 83, 30753084.CrossRefGoogle ScholarPubMed
Silva, LA and Dermody, TS (2017) Chikungunya virus: epidemiology, replication, disease mechanisms, and prospective intervention strategies. Journal of Clinical Investigation 127, 737749.CrossRefGoogle ScholarPubMed
Nayak, TK et al. (2019) p38 and JNK mitogen-activated protein kinases interact with chikungunya virus non-structural protein-2 and regulate TNF induction during viral infection in macrophages. Frontiers in Immunology 10, 786.CrossRefGoogle ScholarPubMed
Varghese, FS et al. (2016) The antiviral alkaloid berberine reduces chikungunya virus-induced mitogen-activated protein kinase signaling. Journal of Virology 90, 97439757.CrossRefGoogle ScholarPubMed
Zell, R (2018) Picornaviridae-the ever-growing virus family. Archives of Virology 163, 299317.CrossRefGoogle ScholarPubMed
Sin, J et al. (2015) Recent progress in understanding coxsackievirus replication, dissemination, and pathogenesis. Virology 484, 288304.CrossRefGoogle ScholarPubMed
Xia, C et al. (2015) Involvement of interleukin 6 in hepatitis B viral infection. Cellular Physiology and Biochemistry 37, 677686.CrossRefGoogle ScholarPubMed
Wei, J et al. (2017) Transcriptional profiling of host cell responses to encephalomyocarditis virus (EMCV). Virology Journal 14, 45.CrossRefGoogle Scholar
Jensen, KJ et al. (2013) An ERK-p38 subnetwork coordinates host cell apoptosis and necrosis during coxsackievirus B3 infection. Cell Host & Microbe 13, 6776.CrossRefGoogle ScholarPubMed
Wu, S et al. (2020) Luteolin inhibits CVB3 replication through inhibiting inflammation. Journal of Asian Natural Products Research 22, 762773.CrossRefGoogle ScholarPubMed
Fu, Q et al. (2019) Scutellaria baicalensis inhibits coxsackievirus B3-induced myocarditis via AKT and p38 pathways. Journal of Microbiology and Biotechnology 29, 12301239.CrossRefGoogle ScholarPubMed
Peng, H et al. (2014) Activation of JNK1/2 and p38 MAPK signaling pathways promotes enterovirus 71 infection in immature dendritic cells. BMC Microbiology 14, 147.CrossRefGoogle ScholarPubMed
Zhang, Z et al. (2017) PD169316, a specific p38 inhibitor, shows antiviral activity against enterovirus71. Virology 508, 150158.CrossRefGoogle ScholarPubMed
Zhu, L et al. (2017) The immune mechanism of intestinal tract Toll-like receptor in mediating EV71 virus type severe hand-foot-and-mouth disease and the MAPK pathway. Experimental and Therapeutic Medicine 13, 22632266.CrossRefGoogle ScholarPubMed
Iordanov, MS et al. (2000) Activation of p38 mitogen-activated protein kinase and c-Jun NH(2)-terminal kinase by double-stranded RNA and encephalomyocarditis virus: involvement of RNase L, protein kinase R, and alternative pathways. Molecular and Cellular Biology 20, 617627.CrossRefGoogle ScholarPubMed
Porter, FW, Brown, B and Palmenberg, AC (2010) Nucleoporin phosphorylation triggered by the encephalomyocarditis virus leader protein is mediated by mitogen-activated protein kinases. Journal of Virology 84, 1253812548.CrossRefGoogle ScholarPubMed
Baseler, L et al. (2017) The pathogenesis of Ebola virus disease. Annual Review of Pathology 12, 387418.CrossRefGoogle ScholarPubMed
Zawilińska, B and Kosz-Vnenchak, M (2014) General introduction into the Ebola virus biology and disease. Folia Medica Cracoviensia 54, 5765.Google ScholarPubMed
Johnson, JC et al. (2014) Pyridinyl imidazole inhibitors of p38 MAP kinase impair viral entry and reduce cytokine induction by Zaire ebolavirus in human dendritic cells. Antiviral Research 107, 102109.CrossRefGoogle ScholarPubMed
Halfmann, P, Neumann, G and Kawaoka, Y (2011) The ebolavirus VP24 protein blocks phosphorylation of p38 mitogen-activated protein kinase. Journal of Infectious Diseases 204(Suppl 3), S953S956.CrossRefGoogle ScholarPubMed
Sharma, V, Mobeen, F and Prakash, T (2016) Comparative genomics of herpesviridae family to look for potential signatures of human infecting strains. International Journal of Genomics 2016, 9543274.CrossRefGoogle ScholarPubMed
Heineman, TC (2007) Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis. Cambridge: Cambridge University Press, pp. 5.Google ScholarPubMed
Song, S et al. (2014) Downregulation of cellular c-Jun N-terminal protein kinase and NF-κB activation by berberine may result in inhibition of herpes simplex virus replication. Antimicrobial Agents and Chemotherapy 58, 50685078.CrossRefGoogle ScholarPubMed
Auerbach, A and Aguilera, NS (2015) Epstein-Barr virus (EBV)-associated lymphoid lesions of the head and neck. Seminars in Diagnostic Pathology 32, 1222.CrossRefGoogle ScholarPubMed
Phan, AT et al. (2016) Epstein-Barr virus latency type and spontaneous reactivation predict lytic induction levels. Biochemical and Biophysical Research Communications 474, 7175.CrossRefGoogle ScholarPubMed
Baird, NL et al. (2013) Varicella zoster virus (VZV)-human neuron interaction. Viruses 5, 21062115.CrossRefGoogle ScholarPubMed
Karaca, G et al. (2004) Inhibition of the stress-activated kinase, p38, does not affect the virus transcriptional program of herpes simplex virus type 1. Virology 329, 142156.CrossRefGoogle Scholar
Zachos, G, Clements, B and Conner, J (1999) Herpes simplex virus type 1 infection stimulates p38/c-Jun N-terminal mitogen-activated protein kinase pathways and activates transcription factor AP-1. Journal of Biological Chemistry 274, 50975103.CrossRefGoogle ScholarPubMed
Hu, S et al. (2011) Reactive oxygen species drive herpes simplex virus (HSV)-1-induced proinflammatory cytokine production by murine microglia. Journal of Neuroinflammation 8, 123.CrossRefGoogle ScholarPubMed
Gonnella, R et al. (2015) PKC theta and p38 MAPK activate the EBV lytic cycle through autophagy induction. Biochimica et Biophysica Acta 1853, 15861595.CrossRefGoogle ScholarPubMed
Park, GB et al. (2014) ROS-mediated JNK/p38-MAPK activation regulates bax translocation in sorafenib-induced apoptosis of EBV-transformed B cells. International Journal of Oncology 44, 977985.CrossRefGoogle ScholarPubMed
Rahaus, M, Desloges, N and Wolff, MH (2004) Replication of varicella-zoster virus is influenced by the levels of JNK/SAPK and p38/MAPK activation. Journal of General Virology 85, 35293540.CrossRefGoogle ScholarPubMed
Rahaus, M, Desloges, N and Wolff, MH (2005) ORF61 protein of varicella-zoster virus influences JNK/SAPK and p38/MAPK phosphorylation. Journal of Medical Virology 76, 424433.CrossRefGoogle ScholarPubMed
Liu, X et al. (2012) Varicella-zoster virus ORF12 protein triggers phosphorylation of ERK1/2 and inhibits apoptosis. Journal of Virology 86, 31433151.CrossRefGoogle ScholarPubMed
Kang, L et al. (2015) Anti-HBV drugs: progress, unmet needs, and new hope. Viruses 7, 49604977.CrossRefGoogle ScholarPubMed
Horng, JH et al. (2020) HBV X protein-based therapeutic vaccine accelerates viral antigen clearance by mobilizing monocyte infiltration into the liver in HBV carrier mice. Journal of Biomedical Science 27, 70.CrossRefGoogle ScholarPubMed
Karayiannis, P (2017) Hepatitis B virus: virology, molecular biology, life cycle and intrahepatic spread. Hepatology International 11, 500508.CrossRefGoogle ScholarPubMed
Tu, W et al. (2019) Hepatitis B virus X protein induces SATB1 expression through activation of ERK and p38 MAPK pathways to suppress anoikis. Digestive Diseases and Sciences 64, 32033214.CrossRefGoogle ScholarPubMed
Chen, Z et al. (2017) Hepatitis B virus core antigen stimulates IL-6 expression via p38, ERK and NF-κB pathways in hepatocytes. Cellular Physiology and Biochemistry 41, 91100.CrossRefGoogle ScholarPubMed
Xiang, WQ et al. (2011) Hepatitis B virus X protein stimulates IL-6 expression in hepatocytes via a MyD88-dependent pathway. Journal of Hepatology 54, 2633.CrossRefGoogle Scholar
Haller, V et al. (2020) An updated patent review of p38 MAP kinase inhibitors (2014–2019). Expert Opinion on Therapeutic Patents 30, 453466.CrossRefGoogle Scholar
Yong, HY, Koh, MS and Moon, A (2009) The p38 MAPK inhibitors for the treatment of inflammatory diseases and cancer. Expert Opinion on Investigational Drugs 18, 18931905.CrossRefGoogle ScholarPubMed
Ye, Q et al. (2020) Ferrostatin-1 mitigates cognitive impairment of epileptic rats by inhibiting p38 MAPK activation. Epilepsy & Behavior: E&B 103, 106670.CrossRefGoogle ScholarPubMed
Cheng, Y et al. (2020) Virus-induced p38 MAPK activation facilitates viral infection. Theranostics 10, 1222312240.CrossRefGoogle ScholarPubMed
Roth, H et al. (2017) Flavivirus infection uncouples translation suppression from cellular stress responses. mBio 8, e02150-16.Google ScholarPubMed
Sreekanth, GP et al. (2016) SB203580 modulates p38 MAPK signaling and dengue virus-induced liver injury by reducing MAPKAPK2, HSP27, and ATF2 phosphorylation. PLoS ONE 11, e0149486.CrossRefGoogle ScholarPubMed
Shen, S et al. (2016) Ion-current-based temporal proteomic profiling of influenza-A-virus-infected mouse lungs revealed underlying mechanisms of altered integrity of the lung microvascular barrier. Journal of Proteome Research 15, 540553.CrossRefGoogle ScholarPubMed
Hui, KP et al. (2009) Induction of proinflammatory cytokines in primary human macrophages by influenza A virus (H5N1) is selectively regulated by IFN regulatory factor 3 and p38 MAPK. Journal of Immunology 182, 10881098.CrossRefGoogle ScholarPubMed
Zhang, Y et al. (2020) Coagulopathy and antiphospholipid antibodies in patients with COVID-19. New England Journal of Medicine 382, e38.CrossRefGoogle ScholarPubMed
Chen, X et al. (2018) Arterial thrombosis is accompanied by elevated mitogen-activated protein kinase (MAPK) and cyclooxygenase-2 (COX-2) expression via Toll-like receptor 4 (TLR-4) activation by S100A8/A9. Medical Science Monitor: International Medical Journal of Experimental and Clinical Research 24, 76737681.CrossRefGoogle ScholarPubMed
Mizutani, T et al. (2004) Phosphorylation of p38 MAPK and its downstream targets in SARS coronavirus-infected cells. Biochemical and Biophysical Research Communications 319, 12281234.CrossRefGoogle ScholarPubMed
Zhou, F et al. (2020) Clinical course and risk factors for mortality of adult inpatients with COVID-19 in Wuhan, China: a retrospective cohort study. Lancet (London, England) 395, 10541062.CrossRefGoogle ScholarPubMed
Cohen, PS et al. (1997) The critical role of p38 MAP kinase in T cell HIV-1 replication. Molecular Medicine 3, 339346.CrossRefGoogle Scholar
Muthumani, K et al. (2004) Suppression of HIV-1 viral replication and cellular pathogenesis by a novel p38/JNK kinase inhibitor. AIDS 18, 739748.CrossRefGoogle ScholarPubMed
Perfettini, JL et al. (2005) Essential role of p53 phosphorylation by p38 MAPK in apoptosis induction by the HIV-1 envelope. Journal of Experimental Medicine 201, 279289.CrossRefGoogle ScholarPubMed
Jafri, M et al. (2007) MAPK signaling contributes to rotaviral-induced cholangiocyte injury and viral replication. Surgery 142, 192201.CrossRefGoogle ScholarPubMed
Si, X et al. (2005) Stress-activated protein kinases are involved in coxsackievirus B3 viral progeny release. Journal of Virology 79, 1387513881.CrossRefGoogle ScholarPubMed
Cao, L et al. (2019) Autophagy induced by enterovirus 71 regulates the production of IL-6 through the p38 MAPK and ERK signaling pathways. Microbial Pathogenesis 131, 120127.CrossRefGoogle ScholarPubMed
Chen, SG et al. (2017) Anti-enterovirus 71 activities of Melissa officinalis extract and its biologically active constituent Rosmarinic acid. Scientific Reports 7, 12264.CrossRefGoogle ScholarPubMed
Leong, SY, Ong, BK and Chu, JJ (2015) The role of misshapen NCK-related kinase (MINK), a novel Ste20 family kinase, in the IRES-mediated protein translation of human enterovirus 71. PLoS Pathogens 11, e1004686.CrossRefGoogle Scholar
Steer, SA et al. (2006) Role of MAPK in the regulation of double-stranded RNA-and encephalomyocarditis virus-induced cyclooxygenase-2 expression by macrophages. Journal of Immunology 177, 34133420.CrossRefGoogle ScholarPubMed
Eliopoulos, AG et al. (1999) Activation of the p38 mitogen-activated protein kinase pathway by Epstein-Barr virus-encoded latent membrane protein 1 coregulates interleukin-6 and interleukin-8 production. Journal of Biological Chemistry 274, 1608516096.CrossRefGoogle ScholarPubMed
Desloges, N et al. (2008) Varicella-zoster virus infection induces the secretion of interleukin-8. Medical Microbiology and Immunology 197, 277284.CrossRefGoogle ScholarPubMed
Adamson, AL et al. (2000) Epstein-Barr virus immediate-early proteins BZLF1 and BRLF1 activate the ATF2 transcription factor by increasing the levels of phosphorylated p38 and c-Jun N-terminal kinases. Journal of Virology 74, 12241233.CrossRefGoogle ScholarPubMed
Liu, X and Cohen, JI (2016) Epstein-Barr Virus (EBV) tegument protein BGLF2 promotes EBV reactivation through activation of the p38 mitogen-activated protein kinase. Journal of Virology 90, 11291138.CrossRefGoogle ScholarPubMed
Huang, W et al. (2012) Herpes simplex virus type 2 infection of human epithelial cells induces CXCL9 expression and CD4+ T cell migration via activation of p38-CCAAT/enhancer-binding protein-β pathway. Journal of Immunology 188, 62476257.CrossRefGoogle ScholarPubMed
Yang, Q et al. (2019) HoxA10 facilitates SHP-1-catalyzed dephosphorylation of p38 MAPK/STAT3 to repress hepatitis B virus replication by a feedback regulatory mechanism. Journal of Virology 93, e01607-18.CrossRefGoogle ScholarPubMed
Zarubin, T and Han, J (2005) Activation and signaling of the p38 MAP kinase pathway. Cell Research 15, 1118.CrossRefGoogle ScholarPubMed
Amatore, D et al. (2015) Influenza virus replication in lung epithelial cells depends on redox-sensitive pathways activated by NOX4-derived ROS. Cellular Microbiology 17, 131145.CrossRefGoogle ScholarPubMed
Li, SW et al. (2016) SARS coronavirus papain-like protease induces Egr-1-dependent up-regulation of TGF-β1 via ROS/p38 MAPK/STAT3 pathway. Scientific Reports 6, 25754.CrossRefGoogle ScholarPubMed
Kopecky-Bromberg, SA, Martinez-Sobrido, L and Palese, P (2006) 7a protein of severe acute respiratory syndrome coronavirus inhibits cellular protein synthesis and activates p38 mitogen-activated protein kinase. Journal of Virology 80, 785793.CrossRefGoogle ScholarPubMed
Muthumani, K et al. (2008) Human immunodeficiency virus type 1 Nef induces programmed death 1 expression through a p38 mitogen-activated protein kinase-dependent mechanism. Journal of Virology 82, 1153611544.CrossRefGoogle ScholarPubMed
Norman, KL et al. (2004) Reovirus oncolysis: the Ras/RalGEF/p38 pathway dictates host cell permissiveness to reovirus infection. Proceedings of the National Academy of Sciences of the USA 101, 1109911104.CrossRefGoogle ScholarPubMed
He, F et al. (2019) The protective role of microRNA-21 against coxsackievirus B3 infection through targeting the MAP2K3/P38 MAPK signaling pathway. Journal of Translational Medicine 17, 335.CrossRefGoogle ScholarPubMed
Zhang, M et al. (2018) Herpes simplex virus type 2 infection-induced expression of CXCR3 ligands promotes CD4(+) T cell migration and is regulated by the viral immediate-early protein ICP4. Frontiers in Immunology 9, 2932.CrossRefGoogle ScholarPubMed
Gillis, PA, Okagaki, LH and Rice, SA (2009) Herpes simplex virus type 1 ICP27 induces p38 mitogen-activated protein kinase signaling and apoptosis in HeLa cells. Journal of Virology 83, 17671777.CrossRefGoogle ScholarPubMed
Li, YX et al. (2016) Hepatitis B virus middle protein enhances IL-6 production via p38 MAPK/NF-κB pathways in an ER stress-dependent manner. PLoS ONE 11, e0159089.Google Scholar