Abstract
The present century will undoubtedly be marked with the COVID-19 global health crisis. It is not time yet to talk about the total number of deaths and hospitalizations, as they are enormously growing daily. Understanding the nature of COVID-19-induced pneumonia is vital in order to deal with the associated health complications. Cell stress is an established mechanism known to be associated with infection and cancer. Different proteins crucial for cellular response to stress are reported to be a possible target to stop the infection and to reduce the chemo-resistance in cancer. Heat shock protein (HSP) families of chaperones play an essential role in cells both in normal state and under stress. The upregulation of HSP5A, also termed GRP78 or Bip, is reported in different viral infections. This chapter introduces the current knowledge about severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which has caused the COVID-19 pandemic, and cell stress aimed at defining possible strategies to combat the COVID-19 pandemic.
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References
Ajiro M, Zheng Z-MJM (2015) E6^ E7, a novel splice isoform protein of human papillomavirus 16, stabilizes viral E6 and E7 oncoproteins via HSP90 and GRP78. mBio 6(1):e02068–e02014
Alexandrescu D, Dutcher J, Wiernik PJ (2005) Metastatic melanoma: is biochemotherapy the future? Med Oncol 22(2):101–111
Andersen KG, Rambaut A, Lipkin WI, Holmes EC, Garry RF (2020) The proximal origin of SARS-CoV-2. Nat Med 26(4):450–452. https://doi.org/10.1038/s41591-020-0820-9
Anguiano L, Riera M, Pascual J, Soler MJ (2017) Circulating ACE2 in cardiovascular and kidney diseases. Curr Med Chem 24(30):3231–3241. https://doi.org/10.2174/0929867324666170414162841
Belouzard S, Millet JK, Licitra BN, Whittaker GR (2012) Mechanisms of coronavirus cell entry mediated by the viral spike protein. Viruses 4(6):1011–1033. https://doi.org/10.3390/v4061011
Bertram S, Glowacka I, Muller MA, Lavender H, Gnirss K, Nehlmeier I, Niemeyer D, He Y, Simmons G, Drosten C, Soilleux EJ, Jahn O, Steffen I, Pohlmann S (2011) Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease. J Virol 85(24):13363–13372. https://doi.org/10.1128/JVI.05300-11
Bhattacharyya S, Hope T (2011) Full-length Ebola glycoprotein accumulates in the endoplasmic reticulum. Virol J 8(1):11
Cha-Molstad H, Yu JE, Feng Z, Lee SH, Kim JG, Yang P, Han B, Sung KW, Yoo YD, Hwang J, McGuire T, Shim SM, Song HD, Ganipisetti S, Wang N, Jang JM, Lee MJ, Kim SJ, Lee KH, Hong JT, Ciechanover A, Mook-Jung I, Kim KP, Xie XQ, Kwon YT, Kim BY (2017) p62/SQSTM1/Sequestosome-1 is an N-recognin of the N-end rule pathway which modulates autophagosome biogenesis. Nat Commun 8(1):102. https://doi.org/10.1038/s41467-017-00085-7
Chan JF, Lau SK, To KK, Cheng VC, Woo PC, Yuen K-Y (2015) Middle East respiratory syndrome coronavirus: another zoonotic betacoronavirus causing SARS-like disease. Clin Microbiol Rev 28(2):465–522
Chan SF, Chen YY, Lin JJ, Liao CL, Ko YC, Tang NY, Kuo CL, Liu KC, Chung JG (2017) Triptolide induced cell death through apoptosis and autophagy in murine leukemia WEHI-3 cells in vitro and promoting immune responses in WEHI-3 generated leukemia mice in vivo. Environ Toxicol 32(2):550–568
Chen T, Xu S (2017) Chronic exposure of cisplatin induces GRP78 expression in ovarian cancer. In: Proceedings of the 2017 4th international conference on biomedical and bioinformatics engineering. ACM, pp 35–38
Chien Y-J, Chen W-J, Hsu W-L, Chiou S-S (2008) Bovine lactoferrin inhibits Japanese encephalitis virus by binding to heparan sulfate and receptor for low density lipoprotein. Virology 379(1):143–151
Chiou SS, Liu H, Chuang CK, Lin CC, Chen WJ (2005) Fitness of Japanese encephalitis virus to Neuro-2a cells is determined by interactions of the viral envelope protein with highly sulfated glycosaminoglycans on the cell surface. J Med Virol 76(4):583–592
Choi Y, Bowman JW, Jung JU (2018) Autophagy during viral infection – a double-edged sword. Nat Rev Microbiol 16(6):341–354. https://doi.org/10.1038/s41579-018-0003-6
Chu H, Chan C-M, Zhang X, Wang Y, Yuan S, Zhou J, Au-Yeung RK-H, Sze K-H, Yang D, Shuai H (2018) Middle East respiratory syndrome coronavirus and bat coronavirus HKU9 both can utilize GRP78 for attachment onto host cells. J Biol Chem 293(30):11709–11726
Cui J, Li F, Shi ZL (2019) Origin and evolution of pathogenic coronaviruses. Nat Rev Microbiol 17(3):181–192. https://doi.org/10.1038/s41579-018-0118-9
de Wit E, van Doremalen N, Falzarano D, Munster VJ (2016) SARS and MERS: recent insights into emerging coronaviruses. Nat Rev Microbiol 14(8):523–534. https://doi.org/10.1038/nrmicro.2016.81
Elfiky AA (2020a) Anti-HCV, nucleotide inhibitors, repurposing against COVID-19. Life Sci 248:117477. https://doi.org/10.1016/j.lfs.2020.117477
Elfiky AA (2020b) Ebola virus glycoprotein GP1-host cell-surface HSPA5 binding site prediction. Cell Stress Chaperones 25(3):541–548. https://doi.org/10.1007/s12192-020-01106-z
Elfiky AA (2020c) Natural products may interfere with SARS-CoV-2 attachment to the host cell. (just-accepted):1–16
Elfiky AA (2020d) Human papillomavirus E6: host cell receptor, GRP78, binding site prediction 92(12):3759-3765. https://doi.org/10.1002/jmv.25737
Elfiky AA (2020e) SARS-CoV-2 Spike-Heat Shock Protein A5 (GRP78) recognition may be related to the immersed human coronaviruses. Frontiers in Pharmacology. (In press). https://doi.org/10.3389/fphar.2020.577467
Elfiky AA, Ibrahim IM (2020) Zika virus envelope – heat shock protein A5 (GRP78) binding site prediction. J Biomol Struct Dyn:1–13. https://doi.org/10.1080/07391102.2020.1784794
Elfiky AA, Mahdy SM, Elshemey WM (2017) Quantitative structure-activity relationship and molecular docking revealed a potency of anti-hepatitis C virus drugs against human corona viruses. J Med Virol 89(6):1040–1047. https://doi.org/10.1002/jmv.24736
Elfiky AA, Ibrahim IM, Ismail AM, Elshemey WM (2020a) A possible role for GRP78 in cross vaccination against COVID-19. Journal of Infection. https://doi.org/10.1016/j.jinf.2020.09.004
Elfiky AA, Baghdady AM, Ali SA, Ahmed MI (2020b) GRP78 targeting: Hitting two birds with a stone. Life Sciences 260:118317. https://doi.org/10.1016/j.lfs.2020.118317Â
Fang L, Karakiulakis G, Roth M (2020) Are patients with hypertension and diabetes mellitus at increased risk for COVID-19 infection? Lancet Respir Med 8(4):e21. https://doi.org/10.1016/S2213-2600(20)30116-8
Feng Y, He D, Yao Z, Klionsky DJ (2014) The machinery of macroautophagy. Cell Res 24(1):24–41. https://doi.org/10.1038/cr.2013.168
Fennelly D, Schneider J (1995) Role of chemotherapy dose intensification in the treatment of advanced ovarian cancer. Oncology 9(10):922
Galluzzi L, Yamazaki T, Kroemer G (2018) Linking cellular stress responses to systemic homeostasis. Nat Rev Mol Cell Biol 19(11):731–745. https://doi.org/10.1038/s41580-018-0068-0
Gething M-J, Sambrook J (1992) Protein folding in the cell 355(6355):33–45
Glowacka I, Bertram S, Muller MA, Allen P, Soilleux E, Pfefferle S, Steffen I, Tsegaye TS, He Y, Gnirss K, Niemeyer D, Schneider H, Drosten C, Pohlmann S (2011) Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response. J Virol 85(9):4122–4134. https://doi.org/10.1128/JVI.02232-10
Ha DP, Van Krieken R, Carlos AJ, Lee AS (2020) The stress-inducible molecular chaperone GRP78 as potential therapeutic target for coronavirus infection. J Infect:S0163-4453(0120)30398-30394. https://doi.org/10.1016/j.jinf.2020.06.017
Haas I (1991) BiP – a heat shock protein involved in immunoglobulin chain assembly. Curr Topics Microbiol Immunol 167:71–82
Hendershot LM, Valentine VA, Lee AS, Morris SW, Shapiro DN (1994) Localization of the gene encoding human BiP/GRP78, the endoplasmic reticulum cognate of the HSP70 family, to chromosome 9q34. Genomics 20(2):281–284. https://doi.org/10.1006/geno.1994.1166
Hilgenfeld R, Peiris M (2013) From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses. Antivir Res 100(1):286–295. https://doi.org/10.1016/j.antiviral.2013.08.015
Hu H, Wang C, Jin Y, Meng Q, Liu Q, Liu Z, Liu K, Liu X, Sun H (2019) Catalpol inhibits homocysteine-induced oxidation and inflammation via inhibiting Nox4/NF-κB and GRP78/PERK pathways in human aorta endothelial cells. Inflammation 42(1):64–80
Huang X, Dong W, Milewska A, Golda A, Qi Y, Zhu QK, Marasco WA, Baric RS, Sims AC, Pyrc K, Li W, Sui J (2015) Human coronavirus HKU1 spike protein uses O-acetylated sialic acid as an attachment receptor determinant and employs hemagglutinin-esterase protein as a receptor-destroying enzyme. J Virol 89(14):7202–7213. https://doi.org/10.1128/JVI.00854-15
Ibrahim IM, Abdelmalek DH, Elfiky AA (2019) GRP78: a cell’s response to stress. Life Sci 226:156–163. https://doi.org/10.1016/j.lfs.2019.04.022
Ibrahim IM, Abdelmalek DH, Elshahat ME, Elfiky AA (2020) COVID-19 spike-host cell receptor GRP78 binding site prediction. J Infect 80(5):554–562. https://doi.org/10.1016/j.jinf.2020.02.026
Ismail AM, Elfiky AA (2020) SARS-CoV-2 spike behavior in situ: a Cryo-EM images for a better understanding of the COVID-19 pandemic. Signal Transduction and Targeted Therapy 5(252)
Ji CH, Kim HY, Heo AJ, Lee SH, Lee MJ, Kim SB, Srinivasrao G, Mun SR, Cha-Molstad H, Ciechanover A, Choi CY, Lee HG, Kim BY, Kwon YT (2019) The N-Degron pathway mediates ER-phagy. Mol Cell 75(5):1058–1072. e1059. https://doi.org/10.1016/j.molcel.2019.06.028
Jindadamrongwech S, Thepparit C, Smith D (2004) Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2. Arch Virol 149(5):915–927
Kaliamurthi S, Selvaraj G, Kaushik AC, Gu K-R, Wei D-Q (2018) Designing of CD8+ and CD8+-overlapped CD4+ epitope vaccine by targeting late and early proteins of human papillomavirus. Biologics 12:107
Kaushik S, Cuervo AM (2018) The coming of age of chaperone-mediated autophagy. Nat Rev Mol Cell Biol 19(6):365–381. https://doi.org/10.1038/s41580-018-0001-6
Kim Y, Lillo AM, Steiniger SC, Liu Y, Ballatore C, Anichini A, Mortarini R, Kaufmann GF, Zhou B, Felding-Habermann B (2006) Targeting heat shock proteins on cancer cells: selection, characterization, and cell-penetrating properties of a peptidic GRP78 ligand. Biochemistry 45(31):9434–9444
Lan J, Ge J, Yu J, Shan S, Zhou H, Fan S, Zhang Q, Shi X, Wang Q, Zhang L, Wang X (2020) Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature 581(7807):215–220. https://doi.org/10.1038/s41586-020-2180-5
Landon LA, Deutscher SL (2003) Combinatorial discovery of tumor targeting peptides using phage display. J Cell Biochem 90(3):509–517
Lee AS (2014) Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential. Nat Rev Cancer 14(4):263–276. https://doi.org/10.1038/nrc3701
Letko M, Marzi A, Munster V (2020) Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses. Nat Microbiol 5(4):562–569. https://doi.org/10.1038/s41564-020-0688-y
Li W, Moore MJ, Vasilieva N, Sui J, Wong SK, Berne MA, Somasundaran M, Sullivan JL, Luzuriaga K, Greenough TC, Choe H, Farzan M (2003) Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426(6965):450–454. https://doi.org/10.1038/nature02145
Li F, Li W, Farzan M, Harrison SC (2005a) Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science (New York, NY) 309(5742):1864–1868. https://doi.org/10.1126/science.1116480
Li W, Shi Z, Yu M, Ren W, Smith C, Epstein JH, Wang H, Crameri G, Hu Z, Zhang H, Zhang J, McEachern J, Field H, Daszak P, Eaton BT, Zhang S, Wang LF (2005b) Bats are natural reservoirs of SARS-like coronaviruses. Science (New York, NY) 310(5748):676–679. https://doi.org/10.1126/science.1118391
Li C, Zhang B, Lv W, Lai C, Chen Z, Wang R, Long X, Feng X (2016) Triptolide inhibits cell growth and GRP78 protein expression but induces cell apoptosis in original and radioresistant NPC cells. Oncotarget 7(31):49588
Lindquist S, Craig E (1988) The heat-shock proteins 22(1):631–677
Little E, Ramakrishnan M, Roy B, Gazit G, Lee AS (1994) The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications. Crit Rev Eukaryotic Gene Exp 4(1):1–18
Luo S, Mao C, Lee B, Lee AS (2006) GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. Mol Cell Biol 26(15):5688–5697
Martinotti S, Ranzato E, Burlando B (2018) (−)-Epigallocatechin-3-gallate induces GRP78 accumulation in the ER and shifts mesothelioma constitutive UPR into proapoptotic ER stress. J Cell Physiol 233(10):7082–7090
Mehrbod P, Ande SR, Alizadeh J, Rahimizadeh S, Shariati A, Malek H, Hashemi M, Glover KKM, Sher AA, Coombs KM, Ghavami S (2019) The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections. Virulence 10(1):376–413. https://doi.org/10.1080/21505594.2019.1605803
Mijaljica D, Prescott M, Devenish RJ (2011) Microautophagy in mammalian cells: revisiting a 40-year-old conundrum. Autophagy 7(7):673–682. https://doi.org/10.4161/auto.7.7.14733
Munro S, Pelham HR (1987) A C-terminal signal prevents secretion of luminal ER proteins. Cell 48(5):899–907
Nain M, Mukherjee S, Karmakar SP, Paton AW, Paton JC, Abdin M, Basu A, Kalia M, Vrati S (2017) GRP78 is an important host factor for Japanese encephalitis virus entry and replication in mammalian cells. J Virol 91(6):e02274–e02216
Ni M, Zhang Y, Lee AS (2011) Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting. Biochem J 434(2):181–188
Niu Z, Wang M, Zhou L, Yao L, Liao Q, Zhao Y (2015) Elevated GRP78 expression is associated with poor prognosis in patients with pancreatic cancer. Sci Rep 5(1):1–12
Ojha CR, Rodriguez M, Lapierre J, Karuppan M, Kumar M, Branscome H, Kashanchi F, El-Hage N (2018) Complementary mechanisms potentially involved in the pathology of Zika virus. Front Immunol 9:2340
Perlman S, Netland J (2009) Coronaviruses post-SARS: update on replication and pathogenesis. Nat Rev Microbiol 7(6):439–450. https://doi.org/10.1038/nrmicro2147
Pfaffenbach KT, Lee AS (2011) The critical role of GRP78 in physiologic and pathologic stress. Curr Opin Cell Biol 23(2):150–156
Raj VS, Mou H, Smits SL, Dekkers DH, Muller MA, Dijkman R, Muth D, Demmers JA, Zaki A, Fouchier RA, Thiel V, Drosten C, Rottier PJ, Osterhaus AD, Bosch BJ, Haagmans BL (2013) Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature 495(7440):251–254. https://doi.org/10.1038/nature12005
Richter K, Haslbeck M, Buchner J (2010) The heat shock response: life on the verge of death. Mol Cell 40(2):253–266. https://doi.org/10.1016/j.molcel.2010.10.006
Samali A, Fulda S, Gorman AM, Hori O, Srinivasula SM (2010) Cell stress and cell death. Int J Cell Biol 2010:245803. https://doi.org/10.1155/2010/245803
Sepulveda D, Rojas-Rivera D, Rodriguez DA, Groenendyk J, Köhler A, Lebeaupin C, Ito S, Urra H, Carreras-Sureda A, Hazari Y (2018) Interactome screening identifies the ER luminal chaperone Hsp47 as a regulator of the unfolded protein response transducer IRE1α. Mol Cell 69(2):238–252. e237
Smit JM, Moesker B, Rodenhuis-Zybert I, Wilschut J (2011) Flavivirus cell entry and membrane fusion. Virus 3(2):160–171
Song W, Gui M, Wang X, Xiang Y (2018) Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. PLoS Pathog 14(8):e1007236. https://doi.org/10.1371/journal.ppat.1007236
South AM, Diz DI, Chappell MC (2020) COVID-19, ACE2, and the cardiovascular consequences. Am J Physiol Heart Circ Physiol 318(5):H1084–H1090. https://doi.org/10.1152/ajpheart.00217.2020
Ting J, Lee AS (1988) Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA 7(4):275–286
Tsai Y-L, Ha DP, Zhao H, Carlos AJ, Wei S, Pun TK, Wu K, Zandi E, Kelly K, Lee AS (2018) Endoplasmic reticulum stress activates SRC, relocating chaperones to the cell surface where GRP78/CD109 blocks TGF-β signaling. Proc Natl Acad Sci U S A 115(18):E4245–E4254
van den Brand JM, Smits SL, Haagmans BL (2015) Pathogenesis of Middle East respiratory syndrome coronavirus. J Pathol 235(2):175–184. https://doi.org/10.1002/path.4458
Vaninov N (2020) In the eye of the COVID-19 cytokine storm. Nat Rev Immunol 20(5):277. https://doi.org/10.1038/s41577-020-0305-6
Wan Y, Shang J, Graham R, Baric RS, Li F (2020) Receptor recognition by the novel coronavirus from Wuhan: an analysis based on decade-long structural studies of SARS coronavirus. J Virol 94(7):e00127–e00120. https://doi.org/10.1128/JVI.00127-20
Wang M, Wey S, Zhang Y, Ye R, Lee AS (2009) Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders. Antioxidants Redox Signal 11(9):2307–2316
Wang N, Shi X, Jiang L, Zhang S, Wang D, Tong P, Guo D, Fu L, Cui Y, Liu X, Arledge KC, Chen YH, Zhang L, Wang X (2013) Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4. Cell Res 23(8):986–993. https://doi.org/10.1038/cr.2013.92
Wu A, Peng Y, Huang B, Ding X, Wang X, Niu P, Meng J, Zhu Z, Zhang Z, Wang J, Sheng J, Quan L, Xia Z, Tan W, Cheng G, Jiang T (2020) Genome composition and divergence of the novel coronavirus (2019-nCoV) originating in China. Cell Host Microbe 27(3):325–328. https://doi.org/10.1016/j.chom.2020.02.001
Xie J, Tao Z-H, Zhao J, Li T, Wu Z-H, Zhang J-F, Zhang J, Hu X-C (2016) Glucose regulated protein 78 (GRP78) inhibits apoptosis and attentinutes chemosensitivity of gemcitabine in breast cancer cell via AKT/mitochondrial apoptotic pathway. Biochem Biophys Res Commun 474(3):612–619
Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q (2020a) Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science (New York, NY) 367(6485):1444–1448. https://doi.org/10.1126/science.abb2762
Yan R, Zhang Y, Li Y, Xia L, Zhou Q (2020b) Structure of dimeric full-length human ACE2 in complex with B0T1. bioRxiv:2020.2002.2017.951848. https://doi.org/10.1101/2020.02.17.951848
Yang L (2020) China confirms human-to-human transmission of coronavirus
Yang J, Chen H, Wang Q, Deng S, Huang M, Ma X, Song P, Du J, Huang Y, Wen Y (2018) Inhibitory effect of kurarinone on growth of human non-small cell lung cancer: an experimental study both in vitro and in vivo studies. Front Pharmacol 9:252
Yeatman TJ (2004) A renaissance for SRC. Nat Rev Cancer 4(6):470–480
Zhang L-Y, Li P-L, Xu A, Zhang X-C (2015) Involvement of GRP78 in the resistance of ovarian carcinoma cells to paclitaxel. Asian Pac J Cancer Prev 16(8):3517–3522
Zhou P, Yang XL, Wang XG, Hu B, Zhang L, Zhang W, Si HR, Zhu Y, Li B, Huang CL, Chen HD, Chen J, Luo Y, Guo H, Jiang RD, Liu MQ, Chen Y, Shen XR, Wang X, Zheng XS, Zhao K, Chen QJ, Deng F, Liu LL, Yan B, Zhan FX, Wang YY, Xiao GF, Shi ZL (2020) A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 579(7798):270–273. https://doi.org/10.1038/s41586-020-2012-7
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Elfiky, A.A., Ibrahim, I.M., Amin, F.G., Ismail, A.M., Elshemey, W.M. (2021). COVID-19 and Cell Stress. In: Rezaei, N. (eds) Coronavirus Disease - COVID-19. Advances in Experimental Medicine and Biology, vol 1318. Springer, Cham. https://doi.org/10.1007/978-3-030-63761-3_10
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