Modulation of endoplasmic reticulum stress response pathways by respiratory viruses

References

• McDonald TP, Jeffree CE, Li P, Rixon HWM, Brown G, Aitken JD, MacLellan K, Sugrue RJ. 2006. Evidence that maturation of the N-linked glycans of the respiratory syncytial virus (RSV) glycoproteins is required for virus-mediated cell fusion: the effect of α-mannosidase inhibitors on RSV infectivity. Virology. 350(2):289–301. doi: 10.1016/j.virol.2006.01.023.
   PubMed Web of Science ®Google Scholar
• Aghaei M, Dastghaib S, Aftabi S, Aghanoori M-R, Alizadeh J, Mokarram P, Mehrbod P, Ashrafizadeh M, Zarrabi A, McAlinden KD, et al. 2020. The ER stress/UPR axis in chronic obstructive pulmonary disease and idiopathic pulmonary fibrosis. Life. 11(1):1. doi: 10.3390/life11010001.
   PubMedGoogle Scholar
• Anderson K, Stott EJ, Wertz GW. 1992. Intracellular processing of the human respiratory syncytial virus fusion glycoprotein: amino acid substitutions affecting folding, transport and cleavage. J Gen Virol. 73(5):1177–1188. doi: 10.1099/0022-1317-73-5-1177.
   PubMedGoogle Scholar
• Andruska N, Zheng X, Yang X, Helferich WG, Shapiro DJ. 2015. Anticipatory estrogen activation of the unfolded protein response is linked to cell proliferation and poor survival in estrogen receptor α-positive breast cancer. Oncogene. 34(29):3760–3769. doi: 10.1038/onc.2014.292.
   PubMed Web of Science ®Google Scholar
• Ao D, Sun S-Q, Guo H-C. 2014. Topology and biological function of enterovirus non-structural protein 2B as a member of the viroporin family. Vet Res. 45(1):87. doi: 10.1186/s13567-014-0087-6.
   PubMedGoogle Scholar
• Aoe T. 2020. Pathological aspects of COVID-19 as a conformational disease and the use of pharmacological chaperones as a potential therapeutic strategy. Front Pharmacol. 11:1095. doi: 10.3389/fphar.2020.01095.
   PubMed Web of Science ®Google Scholar
• Atreya PL, Peeples ME, Collins PL. 1998. The NS1 protein of human respiratory syncytial virus is a potent inhibitor of minigenome transcription and RNA replication. J Virol. 72(2):1452–1461. doi: 10.1128/JVI.72.2.1452-1461.1998.
   PubMed Web of Science ®Google Scholar
• Bahar E, Kim H, Yoon H. 2016. ER stress-mediated signaling: action potential and Ca2+ as key players. Int J Mol Sci. 17(9):1558. doi: 10.3390/ijms17091558.
   PubMed Web of Science ®Google Scholar
• Balakrishnan B, Lai K. 2021. Modulation of SARS-CoV-2 spike-induced unfolded protein response (UPR) in HEK293T cells by selected small chemical molecules. bioRxiv. doi: 10.1101/2021.02.04.429769.
   Google Scholar
• Banerjee AK, Blanco MR, Bruce EA, Honson DD, Chen LM, Chow A, Bhat P, Ollikainen N, Quinodoz SA, Loney C, et al. 2020. SARS-CoV-2 disrupts splicing, translation, and protein trafficking to suppress host defenses. Cell. 183(5):1325–1339.e21. doi: 10.1016/j.cell.2020.10.004.
   PubMed Web of Science ®Google Scholar
• Bao D, Xue R, Zhang M, Lu C, Ma T, Ren C, Zhang T, Yang J, Teng Q, Li X, et al. 2021. N-linked glycosylation plays an important role in budding of neuraminidase protein and virulence of influenza viruses. J Virol. 95(3):e02042-20. doi: 10.1128/JVI.02042-20.
   PubMed Web of Science ®Google Scholar
• Barabutis N. 2020. Unfolded protein response in lung health and disease. Front Med. 7:344. doi: 10.3389/fmed.2020.00344.
   PubMed Web of Science ®Google Scholar
• Bartolini D, Stabile AM, Vacca C, Pistilli A, Rende M, Gioiello A, Cruciani G, Galli F. 2022. Endoplasmic reticulum stress and NF-kB activation in SARS-CoV-2 infected cells and their response to antiviral therapy. IUBMB Life. 74(1):93–100. doi: 10.1002/iub.2537.
   PubMed Web of Science ®Google Scholar
• Bartoszewska S, Collawn JF. 2020. Unfolded protein response (UPR) integrated signaling networks determine cell fate during hypoxia. Cell Mol Biol Lett. 25(1):18. doi: 10.1186/s11658-020-00212-1.
   PubMed Web of Science ®Google Scholar
• Bechill J, Chen Z, Brewer JW, Baker SC. 2008. Coronavirus infection modulates the unfolded protein response and mediates sustained translational repression. J Virol. 82(9):4492–4501. doi: 10.1128/JVI.00017-08.
   PubMed Web of Science ®Google Scholar
• Benton DJ, Wrobel AG, Xu P, Roustan C, Martin SR, Rosenthal PB, Skehel JJ, Gamblin SJ. 2020. Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion. Nature. 588(7837):327–330. doi: 10.1038/s41586-020-2772-0.
   PubMed Web of Science ®Google Scholar
• Bercovich-Kinori A, Tai J, Gelbart IA, Shitrit A, Ben-Moshe S, Drori Y, Itzkovitz S, Mandelboim M, Stern-Ginossar N. 2016. A systematic view on influenza induced host shutoff. Elife. 5:e18311. doi: 10.7554/eLife.18311.
   PubMed Web of Science ®Google Scholar
• Bitko V, Barik S. 2001. An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells by respiratory syncytial virus. J Cell Biochem. 80(3):441–454. doi: 10.1002/1097-4644(20010301)80:3<441::AID-JCB170>3.0.CO;2-C.
   PubMed Web of Science ®Google Scholar
• Boncristiani HF, Criado MF, Arruda E. 2009. Respiratory viruses. In: Schaechter M, editor. Encyclopedia of microbiology. 3rd ed. Oxford: Academic Press; p. 500–518.
   Google Scholar
• Bonifacio JPPL, Williams N, Garnier L, Hugues S, Schmolke M, Mazel-Sanchez B. 2022. Optimizing the live attenuated influenza A vaccine backbone for high-risk patient groups. J Virol. 96(20):e00871-22. doi: 10.1128/jvi.00871-22.
   PubMed Web of Science ®Google Scholar
• Buehler J, Navi D, Lorusso A, Vincent A, Lager K, Miller CL. 2013. Influenza A virus PB1-F2 protein expression is regulated in a strain-specific manner by sequences located downstream of the PB1-F2 initiation codon. J Virol. 87(19):10687–10699. doi: 10.1128/JVI.01520-13.
   PubMed Web of Science ®Google Scholar
• Bukreyev A, Whitehead SS, Murphy BR, Collins PL. 1997. Recombinant respiratory syncytial virus from which the entire SH gene has been deleted grows efficiently in cell culture and exhibits site-specific attenuation in the respiratory tract of the mouse. J Virol. 71(12):8973–8982. doi: 10.1128/jvi.71.12.8973-8982.1997.
   PubMed Web of Science ®Google Scholar
• Byun H, Gou Y, Zook A, Lozano MM, Dudley JP. 2014. ERAD and how viruses exploit it. Front Microbiol. 5:330–20140703. doi: 10.3389/fmicb.2014.00330.
   PubMed Web of Science ®Google Scholar
• Carlos AJ, Ha DP, Yeh D-W, Van Krieken R, Tseng C-C, Zhang P, Gill P, Machida K, Lee AS. 2021. The chaperone GRP78 is a host auxiliary factor for SARS-CoV-2 and GRP78 depleting antibody blocks viral entry and infection. J Biol Chem. 296:100759. doi: 10.1016/j.jbc.2021.100759.
   PubMed Web of Science ®Google Scholar
• Carreras-Sureda A, Pihán P, Hetz C. 2018. Calcium signaling at the endoplasmic reticulum: fine-tuning stress responses. Cell Calcium. 70:24–31. doi: 10.1016/j.ceca.2017.08.004.
   PubMed Web of Science ®Google Scholar
• Castaño-Rodriguez C, Honrubia JM, Gutiérrez-Álvarez J, DeDiego ML, Nieto-Torres JL, Jimenez-Guardeño JM, Regla-Nava JA, Fernandez-Delgado R, Verdia-Báguena C, Queralt-Martín M, et al. 2018. Role of severe acute respiratory syndrome coronavirus viroporins E, 3a, and 8a in replication and pathogenesis. mBio. 9(3):e02325-17. doi: 10.1128/mBio.02325-17.
   PubMed Web of Science ®Google Scholar
• Cervantes-Ortiz SL, Zamorano Cuervo N, Grandvaux N. 2016. Respiratory syncytial virus and cellular stress responses: impact on replication and physiopathology. Viruses. 8(5):124. doi: 10.3390/v8050124.
   PubMed Web of Science ®Google Scholar
• Chamberlain N, Anathy V. 2020. Pathological consequences of the unfolded protein response and downstream protein disulphide isomerases in pulmonary viral infection and disease. J Biochem. 167(2):173–184. doi: 10.1093/jb/mvz101.
   PubMed Web of Science ®Google Scholar
• Chan C-P, Siu K-L, Chin K-T, Yuen K-Y, Zheng B, Jin D-Y. 2006. Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein. J Virol. 80(18):9279–9287. doi: 10.1128/JVI.00659-06.
   PubMed Web of Science ®Google Scholar
• Chen AC-H, Burr L, McGuckin MA. 2018. Oxidative and endoplasmic reticulum stress in respiratory disease. Clin Transl Immunology. 7(6):e1019. doi: 10.1002/cti2.1019.
   PubMed Web of Science ®Google Scholar
• Chen Y, Brandizzi F. 2013. IRE1: ER stress sensor and cell fate executor. Trends Cell Biol. 23(11):547–555. doi: 10.1016/j.tcb.2013.06.005.
   PubMed Web of Science ®Google Scholar
• Cheng S-B, Nakashima A, Huber WJ, Davis S, Banerjee S, Huang Z, Saito S, Sadovsky Y, Sharma S. 2019. Pyroptosis is a critical inflammatory pathway in the placenta from early onset preeclampsia and in human trophoblasts exposed to hypoxia and endoplasmic reticulum stressors. Cell Death Dis. 10(12):927. doi: 10.1038/s41419-019-2162-4.
   PubMedGoogle Scholar
• Chu H, Chan C-M, Zhang X, Wang Y, Yuan S, Zhou J, Au-Yeung RK-H, Sze K-H, Yang D, Shuai H, et al. 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. doi: 10.1074/jbc.RA118.001897.
   PubMed Web of Science ®Google Scholar
• Chu H, Shuai H, Hou Y, Zhang X, Wen L, Huang X, Hu B, Yang D, Wang Y, Yoon C, et al. 2021. Targeting highly pathogenic coronavirus-induced apoptosis reduces viral pathogenesis and disease severity. Sci Adv. 7(25):eabf8577. doi: 10.1126/sciadv.abf8577.
   PubMed Web of Science ®Google Scholar
• Cirone M. 2021. ER stress, UPR activation and the inflammatory response to viral infection. Viruses-Basel. 13(5): 798. doi: 10.3390/v13050798.
   PubMed Web of Science ®Google Scholar
• Collins PL, Hill MG, Cristina J, Grosfeld H. 1996. Transcription elongation factor of respiratory syncytial virus, a nonsegmented negative-strand RNA virus. Proc Natl Acad Sci U S A. 93(1):81–85. doi: 10.1073/pnas.93.1.81.
   PubMed Web of Science ®Google Scholar
• Collins PL, Mottet G. 1991. Post-translational processing and oligomerization of the fusion glycoprotein of human respiratory syncytial virus. J Gen Virol. 72(12):3095–3101. doi: 10.1099/0022-1317-72-12-3095.
   PubMedGoogle Scholar
• Cueno ME, Imai K. 2020. Structural comparison of the SARS CoV 2 spike protein relative to other human-infecting coronaviruses. Front Med. 7:594439. doi: 10.3389/fmed.2020.594439.
   Web of Science ®Google Scholar
• Cui B, Zhang D, Pan H, Zhang F, Farrar J, Law F, van Doorn HR, Wu B, Ba-Thein W. 2015. Viral aetiology of acute respiratory infections among children and associated meteorological factors in southern China. BMC Infect Dis. 15(1):124. doi: 10.1186/s12879-015-0863-6.
   PubMed Web of Science ®Google Scholar
• Davies JP, Sivadas A, Keller KR, Wojcikiewicz RJH, Plate L. 2023. SARS-CoV-2 nonstructural proteins 3 and 4 tune the unfolded protein response. bioRxiv. doi: 10.1101/2023.04.22.537917.
   Google Scholar
• de Almeida SF, Fleming JV, Azevedo JE, Carmo-Fonseca M, de Sousa M. 2007. Stimulation of an Unfolded Protein Response Impairs MHC Class I Expression1. J Immunol. 178(6):3612–3619. doi: 10.4049/jimmunol.178.6.3612.
   PubMed Web of Science ®Google Scholar
• DeDiego ML, Nieto-Torres JL, Jiménez-Guardeño JM, Regla-Nava JA, Alvarez E, Oliveros JC, Zhao J, Fett C, Perlman S, Enjuanes L, et al. 2011. Severe acute respiratory syndrome coronavirus envelope protein regulates cell stress response and apoptosis. PLoS Pathog. 7(10):e1002315. doi: 10.1371/journal.ppat.1002315.
   PubMed Web of Science ®Google Scholar
• Deshpande KL, Fried VA, Ando M, Webster RG. 1987. Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence. Proc Natl Acad Sci U S A. 84(1):36–40. doi: 10.1073/pnas.84.1.36.
   PubMed Web of Science ®Google Scholar
• Dewal MB, DiChiara AS, Antonopoulos A, Taylor RJ, Harmon CJ, Haslam SM, Dell A, Shoulders MD. 2015. XBP1s links the unfolded protein response to the molecular architecture of mature N-glycans. Chem Biol. 22(10):1301–1312. doi: 10.1016/j.chembiol.2015.09.006.
   PubMedGoogle Scholar
• Echavarría-Consuegra L, Cook GM, Busnadiego I, Lefèvre C, Keep S, Brown K, Doyle N, Dowgier G, Franaszek K, Moore NA, et al. 2021. Manipulation of the unfolded protein response: a pharmacological strategy against coronavirus infection. PLoS Pathog. 17(6):e1009644. doi: 10.1371/journal.ppat.1009644.
   PubMed Web of Science ®Google Scholar
• Favreau DJ, Desforges M, St-Jean JR, Talbot PJ. 2009. A human coronavirus OC43 variant harboring persistence-associated mutations in the S glycoprotein differentially induces the unfolded protein response in human neurons as compared to wild-type virus. Virology. 395(2):255–267. doi: 10.1016/j.virol.2009.09.026.
   PubMed Web of Science ®Google Scholar
• Flynn GC, Pohl J, Flocco MT, Rothman JE. 1991. Peptide-binding specificity of the molecular chaperone BiP. Nature. 353(6346):726–730. doi: 10.1038/353726a0.
   PubMed Web of Science ®Google Scholar
• Frabutt DA, Wang B, Riaz S, Schwartz RC, Zheng Y-H, Schultz-Cherry S. 2018. Innate sensing of influenza A virus hemagglutinin glycoproteins by the host endoplasmic reticulum (ER) stress pathway triggers a potent antiviral response via ER-associated protein degradation. J Virol. 92(1):e01690-17. doi: 10.1128/JVI.01690-17.
   PubMed Web of Science ®Google Scholar
• Frabutt DA, Zheng Y-H. 2016. Arms race between enveloped viruses and the host ERAD machinery. Viruses. 8(9):255. doi: 10.3390/v8090255.
   PubMed Web of Science ®Google Scholar
• Fuentes S, Tran KC, Luthra P, Teng MN, He B. 2007. Function of the respiratory syncytial virus small hydrophobic protein. J Virol. 81(15):8361–8366. doi: 10.1128/JVI.02717-06.
   PubMed Web of Science ®Google Scholar
• Fung TS, Liu DX. 2019. Human coronavirus: host-pathogen interaction. Annu Rev Microbiol. 73(1):529–557. doi: 10.1146/annurev-micro-020518-115759.
   PubMed Web of Science ®Google Scholar
• Fung TS, Torres J, Liu DX. 2015. The emerging roles of viroporins in ER stress response and autophagy induction during virus infection. Viruses. 7(6):2834–2857. doi: 10.3390/v7062749.
   PubMed Web of Science ®Google Scholar
• Giurgea LT, Cervantes-Medina A, Walters K-A, Scherler K, Han A, Czajkowski LM, Baus HA, Hunsberger S, Klein SL, Kash JC, et al. 2022. Sex differences in influenza: the challenge study experience. J Infect Dis. 225(4):715–722. doi: 10.1093/infdis/jiab422.
   PubMed Web of Science ®Google Scholar
• Givord C, Welsby I, Detienne S, Thomas S, Assabban A, Lima Silva V, Molle C, Gineste R, Vermeersch M, Perez-Morga D, et al. 2018. Activation of the endoplasmic reticulum stress sensor IRE1α by the vaccine adjuvant AS03 contributes to its immunostimulatory properties. NPJ Vaccines. 3(1):20. doi: 10.1038/s41541-018-0058-4.
   PubMedGoogle Scholar
• Gonzalez-Gronow M, Selim MA, Papalas J, Pizzo SV. 2009. GRP78: a multifunctional receptor on the cell surface. Antioxid Redox Signal. 11(9):2299–2306. doi: 10.1089/ars.2009.2568.
   PubMed Web of Science ®Google Scholar
• Goodman AG, Smith JA, Balachandran S, Perwitasari O, Proll SC, Thomas MJ, Korth MJ, Barber GN, Schiff LA, Katze MG. 2007. The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism. J Virol. 81(5):2221–2230. doi: 10.1128/JVI.02151-06.
   PubMed Web of Science ®Google Scholar
• Grant OC, Montgomery D, Ito K, Woods RJ. 2020. Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition. Sci Rep. 10(1):14991. doi: 10.1038/s41598-020-71748-7.
   PubMed Web of Science ®Google Scholar
• Grey MJ, Cloots E, Simpson MS, LeDuc N, Serebrenik YV, De Luca H, De Sutter D, Luong P, Thiagarajah JR, Paton AW, et al. 2020. IRE1β negatively regulates IRE1α signaling in response to endoplasmic reticulum stress. J Cell Biol. 219(2):e201904048. doi: 10.1083/jcb.201904048.
   PubMed Web of Science ®Google Scholar
• Han D, Lerner AG, Vande Walle L, Upton J-P, Xu W, Hagen A, Backes BJ, Oakes SA, Papa FR. 2009. IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell. 138(3):562–575. doi: 10.1016/j.cell.2009.07.017.
   PubMed Web of Science ®Google Scholar
• Han L, Chen C, Han X, Lin S, Ao X, Han X, Wang J, Ye H. 2019. Structural insights for anti-influenza vaccine design. Comput Struct Biotechnol J. 17:475–483. doi: 10.1016/j.csbj.2019.03.009.
   PubMed Web of Science ®Google Scholar
• Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D. 2000. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell. 5(5):897–904. doi: 10.1016/S1097-2765(00)80330-5.
   PubMed Web of Science ®Google Scholar
• Hassan I, Gaines KS, Hottel WJ, Wishy RM, Miller SE, Powers LS, Rutkowski DT, Monick MM. 2014. Inositol-requiring enzyme 1 inhibits respiratory syncytial virus replication. J Biol Chem. 289(11):7537–7546. doi: 10.1074/jbc.M113.510594.
   PubMed Web of Science ®Google Scholar
• Hassan IH, Zhang MS, Powers LS, Shao JQ, Baltrusaitis J, Rutkowski DT, Legge K, Monick MM. 2012. Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway. J Biol Chem. 287(7):4679–4689. doi: 10.1074/jbc.m111.284695.
   PubMed Web of Science ®Google Scholar
• Haze K, Yoshida H, Yanagi H, Yura T, Mori K. 1999. Mammalian transcription factor ATF6 Is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell. 10(11):3787–3799. doi: 10.1091/mbc.10.11.3787.
   PubMed Web of Science ®Google Scholar
• Hebert DN, Zhang J-X, Chen W, Foellmer B, Helenius A. 1997. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J Cell Biol. 139(3):613–623. doi: 10.1083/jcb.139.3.613.
   PubMed Web of Science ®Google Scholar
• Heikkinen T, Järvinen A. 2003. The common cold. Lancet. 361(9351):51–59. doi: 10.1016/s0140-6736(03)12162-9.
   PubMed Web of Science ®Google Scholar
• Heindel DW, Koppolu S, Zhang Y, Kasper B, Meche L, Vaiana CA, Bissel SJ, Carter CE, Kelvin AA, Elaish M, et al. 2020. Glycomic analysis of host response reveals high mannose as a key mediator of influenza severity. Proc Natl Acad Sci U S A. 117(43):26926–26935. doi: 10.1073/pnas.2008203117.
   PubMed Web of Science ®Google Scholar
• Henkel M, Mitzner D, Henklein P, Meyer-Almes F-J, Moroni A, Difrancesco ML, Henkes LM, Kreim M, Kast SM, Schubert U, et al. 2010. The proapoptotic influenza A virus protein PB1-F2 forms a nonselective ion channel. PLoS One. 5(6):e11112. doi: 10.1371/journal.pone.0011112.
   PubMed Web of Science ®Google Scholar
• Hetz C. 2012. The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol. 13(2):89–102. doi: 10.1038/nrm3270.
   PubMed Web of Science ®Google Scholar
• Hoffman SM, Tully JE, Nolin JD, Lahue KG, Goldman DH, Daphtary N, Aliyeva M, Irvin CG, Dixon AE, Poynter ME, et al. 2013. Endoplasmic reticulum stress mediates house dust mite-induced airway epithelial apoptosis and fibrosis. Respir Res. 14(1):141. doi: 10.1186/1465-9921-14-141.
   PubMed Web of Science ®Google Scholar
• Hollien J, Lin JH, Li H, Stevens N, Walter P, Weissman JS. 2009. Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J Cell Biol. 186(3):323–331. doi: 10.1083/jcb.200903014.
   PubMed Web of Science ®Google Scholar
• Hrincius ER, Liedmann S, Finkelstein D, Vogel P, Gansebom S, Samarasinghe AE, You D, Cormier SA, McCullers JA. 2015. Acute lung injury results from innate sensing of viruses by an ER stress pathway. Cell Rep. 11(10):1591–1603. doi: 10.1016/j.celrep.2015.05.012.
   PubMed Web of Science ®Google Scholar
• Hsu ACY, Wang G, Reid AT, Veerati PC, Pathinayake PS, Daly K, et al. 2020. SARS-CoV-2 spike protein promotes hyper-inflammatory response that can be ameliorated by spike-antagonistic peptide and FDA-approved ER stress and MAP kinase inhibitors in vitro. bioRxiv. doi: 10.1101/2020.09.30.317818.
   Google Scholar
• Hu M, Bogoyevitch MA, Jans DA. 2020. Impact of respiratory syncytial virus infection on host functions: implications for antiviral strategies. Physiol Rev. 100(4):1527–1594. doi: 10.1152/physrev.00030.2019.
   PubMed Web of Science ®Google Scholar
• Huang R, Huestis M, Gan ES, Ooi EE, Ohh M. 2021. Hypoxia and viral infectious diseases. JCI Insight. 6(7):e147190. doi: 10.1172/jci.insight.147190.
   PubMed Web of Science ®Google Scholar
• Huang Y, Yang C, Xu X-f, Xu W, Liu S-w 2020. Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19. Acta Pharmacol Sin. 41(9):1141–1149. doi: 10.1038/s41401-020-0485-4.
   PubMed Web of Science ®Google Scholar
• Ibrahim IM, Abdelmalek DH, Elfiky AA. 2019. GRP78: a cell’s response to stress. Life Sci. 226:156–163. doi: 10.1016/j.lfs.2019.04.022.
   PubMed Web of Science ®Google Scholar
• Jepsen MT, Trebbien R, Emborg HD, Krause TG, Schønning K, Voldstedlund M, Nielsen J, Fischer TK. 2018. Incidence and seasonality of respiratory syncytial virus hospitalisations in young children in Denmark, 2010 to 2015. Euro Surveill. 23(3):17-00163. doi: 10.2807/1560-7917.Es.2018.23.3.17-00163.
   PubMedGoogle Scholar
• Jung KI, Ko D-H, Shin N, Pyo CW, Choi S-Y. 2019. Endoplasmic reticulum-associated degradation potentiates the infectivity of influenza A virus by regulating the host redox state. Free Radic Biol Med. 135:293–305. doi: 10.1016/j.freeradbiomed.2019.03.021.
   PubMed Web of Science ®Google Scholar
• Kaur N, Singh R, Dar Z, Bijarnia RK, Dhingra N, Kaur T. 2021. Genetic comparison among various coronavirus strains for the identification of potential vaccine targets of SARS-CoV2. Infect Genet Evol. 89:104490. doi: 10.1016/j.meegid.2020.104490.
   PubMed Web of Science ®Google Scholar
• Kawasaki N, Asada R, Saito A, Kanemoto S, Imaizumi K. 2012. Obesity-induced endoplasmic reticulum stress causes chronic inflammation in adipose tissue. Sci Rep. 2(1):799. doi: 10.1038/srep00799.
   PubMed Web of Science ®Google Scholar
• Kern DM, Sorum B, Mali SS, Hoel CM, Sridharan S, Remis JP, Toso DB, Kotecha A, Bautista DM, Brohawn SG, et al. 2021. Cryo-EM structure of SARS-CoV-2 ORF3a in lipid nanodiscs. Nat Struct Mol Biol. 28(7):573–582. doi: 10.1038/s41594-021-00619-0.
   PubMed Web of Science ®Google Scholar
• Kim JI, Park MS. 2012. N-linked glycosylation in the hemagglutinin of influenza A viruses. Yonsei Med J. 53(5):886–893. doi: 10.3349/ymj.2012.53.5.886.
   PubMed Web of Science ®Google Scholar
• Kim P, Jang YH, Kwon SB, Lee CM, Han G, Seong BL. 2018. Glycosylation of hemagglutinin and neuraminidase of influenza A virus as signature for ecological spillover and adaptation among influenza reservoirs. Viruses. 10(4):183. doi: 10.3390/v10040183.
   PubMed Web of Science ®Google Scholar
• Kim S, Joe Y, Surh YJ, Chung HT. 2018. Differential regulation of toll-like receptor-mediated cytokine production by unfolded protein response. Oxid Med Cell Longev. 2018:9827312–9827318. doi: 10.1155/2018/9827312.
   PubMed Web of Science ®Google Scholar
• Kimata Y, Ishiwata-Kimata Y, Ito T, Hirata A, Suzuki T, Oikawa D, Takeuchi M, Kohno K. 2007. Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J Cell Biol. 179(1):75–86. doi: 10.1083/jcb.200704166.
   PubMed Web of Science ®Google Scholar
• Kopp MC, Larburu N, Durairaj V, Adams CJ, Ali MMU. 2019. UPR proteins IRE1 and PERK switch BiP from chaperone to ER stress sensor. Nat Struct Mol Biol. 26(11):1053–1062. doi: 10.1038/s41594-019-0324-9.
   PubMed Web of Science ®Google Scholar
• Köseler A, Sabirli R, Gören T, Türkçüer İ, Kurt Ö. 2020. Endoplasmic reticulum stress markers in SARS-COV-2 infection and pneumonia: case-control study. In Vivo. 34(3 suppl):1645–1650. doi: 10.21873/invivo.11956.
   PubMedGoogle Scholar
• Kosik I, Yewdell JW. 2019. Influenza hemagglutinin and neuraminidase: Yin-Yang proteins coevolving to thwart immunity. Viruses. 11(4):346. doi: 10.3390/v11040346.
   PubMed Web of Science ®Google Scholar
• Koutsakos M, McWilliam HEG, Aktepe TE, Fritzlar S, Illing PT, Mifsud NA, Purcell AW, Rockman S, Reading PC, Vivian JP, et al. 2019. Downregulation of MHC Class I expression by influenza A and B viruses. Front Immunol. 10:1158. doi: 10.3389/fimmu.2019.01158.
   PubMed Web of Science ®Google Scholar
• Kozlov G, Gehring K. 2020. Calnexin cycle – structural features of the ER chaperone system. Febs J. 287(20):4322–4340. doi: 10.1111/febs.15330.
   PubMed Web of Science ®Google Scholar
• Kozutsumi Y, Segal M, Normington K, Gething M-J, Sambrook J. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature. 332(6163):462–464. doi: 10.1038/332462a0.
   PubMed Web of Science ®Google Scholar
• Landeras-Bueno S, Fernández Y, Falcón A, Oliveros JC, Ortín J, Kawaoka Y, et al. 2016. Chemical genomics identifies the PERK-mediated unfolded protein stress response as a cellular target for influenza virus inhibition. mBio. 7(2):e00085-16–e00016. doi: 10.1128/mBio.00085-16.
   PubMed Web of Science ®Google Scholar
• Lee AH, Iwakoshi NN, Glimcher LH. 2003. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol. 23(21):7448–7459. doi: 10.1128/mcb.23.21.7448-7459.2003.
   PubMed Web of Science ®Google Scholar
• Leymarie O, Embury-Hyatt C, Chevalier C, Jouneau L, Moroldo M, Da Costa B, Berhane Y, Delmas B, Weingartl HM, Le Goffic R, et al. 2014. PB1-F2 attenuates virulence of highly pathogenic avian H5N1 influenza virus in chickens. PLoS One. 9(6):e100679. doi: 10.1371/journal.pone.0100679.
   PubMed Web of Science ®Google Scholar
• Li Y, Jain N, Limpanawat S, To J, Quistgaard EM, Nordlund P, Thanabalu T, Torres J. 2015. Interaction between human BAP31 and respiratory syncytial virus small hydrophobic (SH) protein. Virology. 482:105–110. doi: 10.1016/j.virol.2015.03.034.
   PubMed Web of Science ®Google Scholar
• Li Y, Liu D, Wang Y, Su W, Liu G, Dong W. 2021. The importance of glycans of viral and host proteins in enveloped virus infection. Front Immunol. 12:638573. doi: 10.3389/fimmu.2021.638573.
   PubMed Web of Science ®Google Scholar
• Li Z, Guo D, Qin Y, Chen M. 2019. PI4KB on inclusion bodies formed by ER membrane remodeling facilitates replication of human parainfluenza virus type 3. Cell Rep. 29(8):2229–2242.e4. doi: 10.1016/j.celrep.2019.10.052.
   PubMed Web of Science ®Google Scholar
• Liu X, Wen Y-Z, Huang Z-L, Shen X, Wang J-H, Luo Y-H, Chen W-X, Lun Z-R, Li H-B, Qu L-H, et al. 2022. SARS-CoV-2 causes a significant stress response mediated by small RNAs in the blood of COVID-19 patients. Mol Ther Nucleic Acids. 27:751–762. doi: 10.1016/j.omtn.2021.12.034.
   PubMedGoogle Scholar
• Lu W, Zheng B-J, Xu K, Schwarz W, Du L, Wong CKL, Chen J, Duan S, Deubel V, Sun B, et al. 2006. Severe acute res­piratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus release. Proc Natl Acad Sci U S A. 103(33):12540–12545. doi: 10.1073/pnas.0605402103.
   PubMed Web of Science ®Google Scholar
• Lu Y, Wambach M, Katze MG, Krug RM. 1995. Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the eIF-2 translation initiation factor. Virology. 214(1):222–228. doi: 10.1006/viro.1995.9937.
   PubMed Web of Science ®Google Scholar
• Ma J, Li S, Li K, Wang X, Li S. 2019. Effects of the PA-X and PB1-F2 proteins on the virulence of the 2009 pandemic H1N1 influenza A virus in mice. Front Cell Infect Microbiol. 9:315. doi: 10.3389/fcimb.2019.00315.
   PubMed Web of Science ®Google Scholar
• Marchant D, Singhera GK, Utokaparch S, Hackett TL, Boyd JH, Luo Z, Si X, Dorscheid DR, McManus BM, Hegele RG, et al. 2010. Toll-like receptor 4-mediated activation of p38 mitogen-activated protein kinase is a determinant of respiratory virus entry and tropism. J Virol. 84(21):11359–11373. doi: 10.1128/JVI.00804-10.
   PubMed Web of Science ®Google Scholar
• Martino MB, Jones L, Brighton B, Ehre C, Abdulah L, Davis CW, Ron D, O'Neal WK, Ribeiro CMP. 2013. The ER stress transducer IRE1β is required for airway epithelial mucin production. Mucosal Immunol. 6(3):639–654. doi: 10.1038/mi.2012.105.
   PubMed Web of Science ®Google Scholar
• Martinon F, Chen X, Lee A-H, Glimcher LH. 2010. TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nat Immunol. 11(5):411–418. doi: 10.1038/ni.1857.
   PubMed Web of Science ®Google Scholar
• Mazel-Sanchez B, Iwaszkiewicz J, Bonifacio JPP, Silva F, Niu C, Strohmeier S, Eletto D, Krammer F, Tan G, Zoete V, et al. 2021. Influenza A viruses balance ER stress with host protein synthesis shutoff. Proc Natl Acad Sci USA. 118(36):e2024681118. doi: 10.1073/pnas.2024681118.
   PubMed Web of Science ®Google Scholar
• McLellan JS, Ray WC, Peeples ME. 2013. Structure and function of respiratory syncytial virus surface glycoproteins. Curr Top Microbiol Immunol. 372:83–104. doi: 10.1007/978-3-642-38919-1_4.
   PubMed Web of Science ®Google Scholar
• McQuiston A, Diehl JA. 2017. Recent insights into PERK-dependent signaling from the stressed endoplasmic reticulum. F1000Res. 6:1897–20171027. doi: 10.12688/f1000research.12138.1.
   PubMedGoogle Scholar
• Mehrbod P, Ande SR, Alizadeh J, Rahimizadeh S, Shariati A, Malek H, Hashemi M, Glover KKM, Sher AA, Coombs KM, et al. 2019. The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections. Virulence. 10(1):376–413. doi: 10.1080/21505594.2019.1605803.
   PubMed Web of Science ®Google Scholar
• Minakshi R, Padhan K, Rani M, Khan N, Ahmad F, Jameel S. 2009. The SARS coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor. PLoS One. 4(12):e8342. doi: 10.1371/journal.pone.0008342.
   PubMed Web of Science ®Google Scholar
• Mo X-T, Zhou W-C, Cui W-H, Li D-L, Li L-C, Xu L, Zhao P, Gao J. 2015. Inositol-requiring protein 1 - X-box-binding protein 1 pathway promotes epithelial-mesenchymal transition via mediating snail expression in pulmonary fibrosis. Int J Biochem Cell Biol. 65:230–238. doi: 10.1016/j.biocel.2015.06.006.
   PubMed Web of Science ®Google Scholar
• Moa AM, Menzies RI, Yin JK, MacIntyre CR. 2022. Modelling the influenza disease burden in people aged 50–64 and ≥65 years in Australia. Influenza Other Respir Viruses. 16(1):132–141. doi: 10.1111/irv.12902.
   PubMed Web of Science ®Google Scholar
• Moghadami M. 2017. A narrative review of influenza: a seasonal and pandemic disease. Iran J Med Sci. 42(1):2–13.
   PubMed Web of Science ®Google Scholar
• Nagy PD, Strating JR, van Kuppeveld FJ. 2016. Building viral replication organelles: close encounters of the membrane types. PLoS Pathog. 12(10):e1005912. doi: 10.1371/journal.ppat.1005912.
   PubMed Web of Science ®Google Scholar
• Nain M, Mukherjee S, Karmakar SP, Paton AW, Paton JC, Abdin MZ, 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):e02274-16. doi: 10.1128/JVI.02274-16.
   PubMed Web of Science ®Google Scholar
• Narayanan S, Elesela S, Rasky AJ, Morris SH, Kumar S, Lombard D, Lukacs NW. 2022. ER stress protein PERK promotes inappropriate innate immune responses and pathogenesis during RSV infection. J Leukoc Biol. 111(2):379–389. doi: 10.1002/JLB.3A0520-322RR.
   PubMed Web of Science ®Google Scholar
• Nguyen LC, Renner DM, Silva D, Yang D, Parenti NA, Medina KM, Nicolaescu V, Gula H, Drayman N, Valdespino A, et al. 2022. SARS-CoV-2 diverges from other betacoronaviruses in only partially activating the IRE1α/XBP1 endoplasmic reticulum stress pathway in human lung-derived cells. mBio. 13(5):e02415-22. doi: 10.1128/mbio.02415-22.
   PubMed Web of Science ®Google Scholar
• Nguyen LC, Yang D, Nicolaescu V, Best TJ, Gula H, Saxena D, Gabbard JD, Chen S-N, Ohtsuki T, Friesen JB, et al. 2022. Cannabidiol inhibits SARS-CoV-2 replication through induction of the host ER stress and innate immune responses. Sci Adv. 8(8):eabi6110. doi: 10.1126/sciadv.abi6110.
   PubMed Web of Science ®Google Scholar
• Numajiri Haruki A, Naito T, Nishie T, Saito S, Nagata K. 2011. Interferon-inducible antiviral protein MxA enhances cell death triggered by endoplasmic reticulum stress. J Interferon Cytokine Res. 31(11):847–856. doi: 10.1089/jir.2010.0132.
   PubMed Web of Science ®Google Scholar
• Oliveira CC, van Hall T. 2015. Alternative antigen processing for MHC class I: multiple roads lead to Rome. Front Immunol. 6:298. doi: 10.3389/fimmu.2015.00298.
   PubMed Web of Science ®Google Scholar
• Oslowski CM, Urano F. 2011. Measuring ER stress and the unfolded protein response using mammalian tissue culture system. Methods Enzymol. 490:71–92. doi: 10.1016/b978-0-12-385114-7.00004-0.
   PubMed Web of Science ®Google Scholar
• Pahl HL, Baeuerle PA. 1996. Activation of NF-κB by ER stress requires both Ca2+ and reactive oxygen intermediates as messengers. FEBS Lett. 392(2):129–136. doi: 10.1016/0014-5793(96)00800-9.
   PubMed Web of Science ®Google Scholar
• Pahl HL, Baeuerle PA. 1997. The ER-overload response: activation of NF-κB. Trends Biochem Sci. 22(2):63–67. doi: 10.1016/S0968-0004(96)10073-6.
   PubMed Web of Science ®Google Scholar
• Pandey VK, Sharma R, Prajapati GK, Mohanta TK, Mishra AK. 2022. N-glycosylation, a leading role in viral infection and immunity development. Mol Biol Rep. 49(8):8109–8120. doi: 10.1007/s11033-022-07359-4.
   PubMed Web of Science ®Google Scholar
• Park S, Lim Y, Lee D, Elvira R, Lee J-M, Lee MR, Han J. 2018. Modulation of protein synthesis by eIF2α phosphorylation protects cell from heat stress-mediated apoptosis. Cells. 7(12):254. doi: 10.3390/cells7120254.
   PubMed Web of Science ®Google Scholar
• Phillips AM, Doud MB, Gonzalez LO, Butty VL, Lin Y-S, Bloom JD, Shoulders MD. 2018. Enhanced ER proteostasis and temperature differentially impact the mutational tolerance of influenza hemagglutinin. Elife. 7:e38795. doi: 10.7554/eLife.38795.
   PubMed Web of Science ®Google Scholar
• Poppe M, Wittig S, Jurida L, Bartkuhn M, Wilhelm J, Müller H, Beuerlein K, Karl N, Bhuju S, Ziebuhr J, et al. 2017. The NF-κB-dependent and -independent transcriptome and chromatin landscapes of human coronavirus 229E-infected cells. PLoS Pathog. 13(3):e1006286. doi: 10.1371/journal.ppat.1006286.
   PubMed Web of Science ®Google Scholar
• Prasad V, Greber UF. 2021. The endoplasmic reticulum unfolded protein response – homeostasis, cell death and evolution in virus infections. FEMS Microbiol Rev. 45(5):1–19. doi: 10.1093/femsre/fuab016.
   Web of Science ®Google Scholar
• Prasad V, Suomalainen M, Jasiqi Y, Hemmi S, Hearing P, Hosie L, Burgert H-G, Greber UF. 2020. The UPR sensor IRE1α and the adenovirus E3-19K glycoprotein sustain persistent and lytic infections. Nat Commun. 11(1):1997. doi: 10.1038/s41467-020-15844-2.
   PubMed Web of Science ®Google Scholar
• Puzyrenko A, Jacobs ER, Sun Y, Felix JC, Sheinin Y, Ge L, Lai S, Dai Q, Gantner BN, Nanchal R, et al. 2021. Pneumocytes are distinguished by highly elevated expression of the ER stress biomarker GRP78, a co-receptor for SARS-CoV-2, in COVID-19 autopsies. Cell Stress Chaperones. 26(5):859–868. doi: 10.1007/s12192-021-01230-4.
   PubMed Web of Science ®Google Scholar
• Qiao D, Skibba M, Xu X, Garofalo RP, Zhao Y, Brasier AR. 2021. Paramyxovirus replication induces the hexosamine biosynthetic pathway and mesenchymal transition via the IRE1α-XBP1s arm of the unfolded protein response. Am J Physiol Lung Cell Mol Physiol. 321(3):L576–L594. doi: 10.1152/ajplung.00127.2021.
   PubMed Web of Science ®Google Scholar
• Rashid F, Dzakah EE, Wang H, Tang S. 2021. The ORF8 protein of SARS-CoV-2 induced endoplasmic reticulum stress and mediated immune evasion by antagonizing production of interferon beta. Virus Res. 296:198350. doi: 10.1016/j.virusres.2021.198350.
   PubMed Web of Science ®Google Scholar
• Ravindran MS, Bagchi P, Cunningham CN, Tsai B. 2016. Opportunistic intruders: how viruses orchestrate ER functions to infect cells. Nat Rev Microbiol. 14(7):407–420. doi: 10.1038/nrmicro.2016.60.
   PubMed Web of Science ®Google Scholar
• Reading PC, Tate MD, Pickett DL, Brooks AG. 2007. Glycosylation as a target for recognition of influenza viruses by the innate immune system. Adv Exp Med Biol. 598:279–292. doi: 10.1007/978-0-387-71767-8_20.
   PubMed Web of Science ®Google Scholar
• Rheinemann L, Sundquist WI. 2021. Virus budding. In: Bamford DH, Zuckerman M, editors. Encyclopedia of virology. 4th ed. Oxford: Academic Press; p. 519–528.
   Google Scholar
• Roberson EC, Tully JE, Guala AS, Reiss JN, Godburn KE, Pociask DA, Alcorn JF, Riches DWH, Dienz O, Janssen-Heininger YMW, et al. 2012. Influenza induces endoplasmic reticulum stress, caspase-12–dependent apoptosis, and c-Jun N-terminal kinase–mediated transforming growth factor–β release in lung epithelial cells. Am J Respir Cell Mol Biol. 46(5):573–581. doi: 10.1165/rcmb.2010-0460OC.
   PubMed Web of Science ®Google Scholar
• Rosa-Fernandes L, Lazari LC, D, Silva JM, De Morais Gomes V, Machado RRG, D, Santos AF, et al. 2021. SARS-CoV-2 activates ER stress and unfolded protein response. bioRxiv. doi: 10.1101/2021.06.21.449284.
   Google Scholar
• Rutkowski DT, Kaufman RJ. 2004. A trip to the ER: coping with stress. Trends Cell Biol. 14(1):20–28. doi: 10.1016/j.tcb.2003.11.001.
   PubMed Web of Science ®Google Scholar
• Ryu W-S. 2017. Chapter 3 – Virus life cycle. In: Ryu W-S, editor. Molecular virology of human pathogenic viruses. Boston: Academic Press; p. 31–45.
   Google Scholar
• Sabirli R, Koseler A, Goren T, Turkcuer I, Kurt O. 2021. High GRP78 levels in Covid-19 infection: a case-control study. Life Sci. 265:118781. doi: 10.1016/j.lfs.2020.118781.
   PubMed Web of Science ®Google Scholar
• Sakaguchi T, Leser GP, Lamb RA. 1996. The ion channel activity of the influenza virus M2 protein affects transport through the Golgi apparatus. J Cell Biol. 133(4):733–747. doi: 10.1083/jcb.133.4.733.
   PubMed Web of Science ®Google Scholar
• Savic M, Penders Y, Shi T, Branche A, Pirçon J-Y. 2023. Respiratory syncytial virus disease burden in adults aged 60 years and older in high-income countries: a systematic literature review and meta-analysis. Influenza Other Respir Viruses. 17(1):e13031. doi: 10.1111/irv.13031.
   PubMed Web of Science ®Google Scholar
• Schmoldt C, Vazquez-Armendariz AI, Shalashova I, Selvakumar B, Bremer CM, Peteranderl C, Wasnick R, Witte B, Gattenlöhner S, Fink L, et al. 2019. IRE1 signaling as a putative therapeutic target in influenza virus–induced pneumonia. Am J Respir Cell Mol Biol. 61(4):537–540. doi: 10.1165/rcmb.2019-0123LE.
   PubMed Web of Science ®Google Scholar
• Schögler A, Caliaro O, Brügger M, Oliveira Esteves BI, Nita I, Gazdhar A, Geiser T, Alves MP. 2019. Modulation of the unfolded protein response pathway as an antiviral approach in airway epithelial cells. Antiviral Res. 162:44–50. doi: 10.1016/j.antiviral.2018.12.007.
   PubMed Web of Science ®Google Scholar
• Schubert K, Karousis ED, Jomaa A, Scaiola A, Echeverria B, Gurzeler L-A, Leibundgut M, Thiel V, Mühlemann O, Ban N, et al. 2020. SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation. Nat Struct Mol Biol. 27(10):959–966. doi: 10.1038/s41594-020-0511-8.
   PubMed Web of Science ®Google Scholar
• Schuck S, Prinz WA, Thorn KS, Voss C, Walter P. 2009. Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. J Cell Biol. 187(4):525–536. doi: 10.1083/jcb.200907074.
   PubMed Web of Science ®Google Scholar
• Schwarz DS, Blower MD. 2016. The endoplasmic reticulum: structure, function and response to cellular signaling. Cell Mol Life Sci. 73(1):79–94. doi: 10.1007/s00018-015-2052-6.
   PubMed Web of Science ®Google Scholar
• Sgarbanti R, Nencioni L, Amatore D, Coluccio P, Fraternale A, Sale P, Mammola CL, Carpino G, Gaudio E, Magnani M, et al. 2011. Redox regulation of the influenza hemagglutinin maturation process: a new cell-mediated strategy for anti-influenza therapy. Antioxid Redox Signal. 15(3):593–606. doi: 10.1089/ars.2010.3512.
   PubMed Web of Science ®Google Scholar
• Shaban MS, Mayr-Buro C, Meier-Soelch J, Albert BV, Schmitz ML, Ziebuhr J, Kracht M. 2022. Thapsigargin: key to new host-directed coronavirus antivirals? Trends Pharmacol Sci. 43(7):557–568. doi: 10.1016/j.tips.2022.04.004.
   PubMed Web of Science ®Google Scholar
• Shaban MS, Müller C, Mayr-Buro C, Weiser H, Meier-Soelch J, Albert BV, Weber A, Linne U, Hain T, Babayev I, et al. 2021. Multi-level inhibition of coronavirus replication by chemical ER stress. Nat Commun. 12(1):5536. doi: 10.1038/s41467-021-25551-1.
   PubMed Web of Science ®Google Scholar
• Shabbir S, Hafeez A, Rafiq MA, Khan MJ. 2020. Estrogen shields women from COVID-19 complications by reducing ER stress. Med Hypotheses. 143:110148. doi: 10.1016/j.mehy.2020.110148.
   PubMed Web of Science ®Google Scholar
• Shen J, Chen X, Hendershot L, Prywes R. 2002. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell. 3(1):99–111. doi: 10.1016/S1534-5807(02)00203-4.
   PubMed Web of Science ®Google Scholar
• Shi C-S, Nabar NR, Huang N-N, Kehrl JH. 2019. SARS-coronavirus open reading frame-8b triggers intracellular stress pathways and activates NLRP3 inflammasomes. Cell Death Discov. 5(1):101. doi: 10.1038/s41420-019-0181-7.
   PubMedGoogle Scholar
• Shu J, Dang L, Zhang D, Shah P, Chen L, Zhang H, Sun S. 2019. Dynamic analysis of proteomic alterations in response to N-linked glycosylation inhibition in a drug-resistant ovarian carcinoma cell line. FEBS J. 286(8):1594–1605. doi: 10.1111/febs.14811.
   PubMed Web of Science ®Google Scholar
• Sims AC, Mitchell HD, Gralinski LE, Kyle JE, Burnum-Johnson KE, Lam M, Fulcher ML, West A, Smith RD, Randell SH, et al. 2021. Unfolded protein response inhibition reduces Middle East Respiratory Syndrome coronavirus-induced acute lung injury. mBio. 12(4):e01572-21. doi: 10.1128/mBio.01572-21.
   PubMed Web of Science ®Google Scholar
• Siri M, Dastghaib S, Zamani M, Rahmani-Kukia N, Geraylow KR, Fakher S, Keshvarzi F, Mehrbod P, Ahmadi M, Mokarram P, et al. 2021. Autophagy, unfolded protein response, and neuropilin-1 cross-talk in SARS-CoV-2 infection: what can be learned from other coronaviruses. Int J Mol Sci. 22(11):5992. doi: 10.3390/ijms22115992.
   PubMed Web of Science ®Google Scholar
• Sitia R, Braakman I. 2003. Quality control in the endoplasmic reticulum protein factory. Nature. 426(6968):891–894. doi: 10.1038/nature02262.
   PubMed Web of Science ®Google Scholar
• Siu K-L, Chan C-P, Kok K-H, C-Y, Woo P, Jin D-Y. 2014. Comparative analysis of the activation of unfolded protein response by spike proteins of severe acute respiratory syndrome coronavirus and human coronavirus HKU1. Cell Biosci. 4(1):3. doi: 10.1186/2045-3701-4-3.
   PubMedGoogle Scholar
• Snijder EJ, Limpens RWAL, de Wilde AH, de Jong AWM, Zevenhoven-Dobbe JC, Maier HJ, Faas FFGA, Koster AJ, Bárcena M. 2020. A unifying structural and functional model of the coronavirus replication organelle: tracking down RNA synthesis. PLoS Biol. 18(6):e3000715. doi: 10.1371/journal.pbio.3000715.
   PubMed Web of Science ®Google Scholar
• Soldà T, Garbi N, Hämmerling GJ, Molinari M. 2006. Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle. J Biol Chem. 281(10):6219–6226. doi: 10.1074/jbc.M513595200.
   PubMed Web of Science ®Google Scholar
• Song J, Chi M, Luo X, Song Q, Xia D, Shi B, Han J. 2019. Non-structural protein 2B of human rhinovirus 16 activates both PERK and ATF6 rather than IRE1 to trigger ER stress. Viruses. 11(2):133. doi: 10.3390/v11020133.
   PubMed Web of Science ®Google Scholar
• Stanley P, Moremen KW, Lewis NE, Taniguchi N, Aebi MN-G. 2022. N-glycans. In: Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, editors. Essentials of glycobiology. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; p. 103–116.
   Google Scholar
• Su WQ, Yu XJ, Zhou CM. 2021. SARS-CoV-2 ORF3a induces incomplete autophagy via the unfolded protein response. Viruses. 13(12):2467. doi: 10.3390/v13122467.
   PubMed Web of Science ®Google Scholar
• Sudhakar M, Winfred SB, Meiyazhagan G, Venkatachalam DP. 2022. Mechanisms contributing to adverse outcomes of COVID-19 in obesity. Mol Cell Biochem. 477(4):1155–1193. doi: 10.1007/s11010-022-04356-w.
   PubMed Web of Science ®Google Scholar
• Sun X, Jayaraman A, Maniprasad P, Raman R, Houser KV, Pappas C, Zeng H, Sasisekharan R, Katz JM, Tumpey TM, et al. 2013. N-linked glycosylation of the hemagglutinin protein influences virulence and antigenicity of the 1918 pandemic and seasonal H1N1 influenza A viruses. J Virol. 87(15):8756–8766. doi: 10.1128/JVI.00593-13.
   PubMed Web of Science ®Google Scholar
• Sung S-C, Chao C-Y, Jeng K-S, Yang J-Y, Lai MMC. 2009. The 8ab protein of SARS-CoV is a luminal ER membrane-associated protein and induces the activation of ATF6. Virology. 387(2):402–413. doi: 10.1016/j.virol.2009.02.021.
   PubMed Web of Science ®Google Scholar
• Tate MD, Job ER, Deng Y-M, Gunalan V, Maurer-Stroh S, Reading PC. 2014. Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection. Viruses. 6(3):1294–1316. doi: 10.3390/v6031294.
   PubMed Web of Science ®Google Scholar
• Taylor RC. 2016. Aging and the UPR(ER). Brain Res. 1648(Pt B):588–593. doi: 10.1016/j.brainres.2016.04.017.
   PubMedGoogle Scholar
• Tirasophon W, Lee K, Callaghan B, Welihinda A, Kaufman RJ. 2000. The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response. Genes Dev. 14(21):2725–2736. doi: 10.1101/gad.839400.
   PubMed Web of Science ®Google Scholar
• To J, Torres J. 2019. Viroporins in the influenza virus. Cells. 8(7):654. doi: 10.3390/cells8070654.
   PubMed Web of Science ®Google Scholar
• Triantafilou K, Fradelizi D, Wilson K, Triantafilou M. 2002. GRP78, a coreceptor for coxsackievirus A9, interacts with major histocompatibility complex class I molecules which mediate virus internalization. J Virol. 76(2):633–643. doi: 10.1128/JVI.76.2.633-643.2002.
   PubMed Web of Science ®Google Scholar
• Triantafilou K, Kar S, Vakakis E, Kotecha S, Triantafilou M. 2013. Human respiratory syncytial virus viroporin SH: a viral recognition pathway used by the host to signal inflammasome activation. Thorax. 68(1):66–75. doi: 10.1136/thoraxjnl-2012-202182.
   PubMed Web of Science ®Google Scholar
• Tsuru A, Fujimoto N, Takahashi S, Saito M, Nakamura D, Iwano M, Iwawaki T, Kadokura H, Ron D, Kohno K, et al. 2013. Negative feedback by IRE1β optimizes mucin production in goblet cells. Proc Natl Acad Sci U S A. 110(8):2864–2869. doi: 10.1073/pnas.1212484110.
   PubMed Web of Science ®Google Scholar
• Tumpey TM, García-Sastre A, Taubenberger JK, Palese P, Swayne DE, Basler CF. 2004. Pathogenicity and immunogenicity of influenza viruses with genes from the 1918 pandemic virus. Proc Natl Acad Sci U S A. 101(9):3166–3171. doi: 10.1073/pnas.0308391100.
   PubMed Web of Science ®Google Scholar
• van Diepen A, Brand HK, Sama I, Lambooy LHJ, van den Heuvel LP, van der Well L, Huynen M, Osterhaus ADME, Andeweg AC, Hermans PWM, et al. 2010. Quantitative proteome profiling of respiratory virus-infected lung epithelial cells. J Proteomics. 73(9):1680–1693. doi: 10.1016/j.jprot.2010.04.008.
   PubMed Web of Science ®Google Scholar
• Verdiá-Báguena C, Nieto-Torres JL, Alcaraz A, DeDiego ML, Torres J, Aguilella VM, Enjuanes L. 2012. Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids. Virology. 432(2):485–494. doi: 10.1016/j.virol.2012.07.005.
   PubMed Web of Science ®Google Scholar
• Versteeg GA, Nes P, Bredenbeek PJ, Spaan WJM. 2007. The coronavirus spike protein induces endoplasmic reticulum stress and upregulation of intracellular chemokine mRNA concentrations. J Virol. 81(20):10981–10990. doi: 10.1128/JVI.01033-07.
   PubMed Web of Science ®Google Scholar
• Walker GJ, Stelzer-Braid S, Shorter C, Honeywill C, Wynn M, Willenborg C, Barnes P, Kang J, Pierse N, Crane J, et al. 2022. Viruses associated with acute respiratory infection in a community-based cohort of healthy New Zealand children. J Med Virol. 94(2):454–460. doi: 10.1002/jmv.25493.
   PubMed Web of Science ®Google Scholar
• Walsh D, Mohr I. 2011. Viral subversion of the host protein synthesis machinery. Nat Rev Microbiol. 9(12):860–875. doi: 10.1038/nrmicro2655.
   PubMed Web of Science ®Google Scholar
• Wang C, Lashua LP, Carter CE, Johnson SK, Wang M, Ross TM, Ghedin E, Zhang B, Forst CV. 2022. Sex disparities in influenza: a multiscale network analysis. iScience. 25(5):104192. doi: 10.1016/j.isci.2022.104192.
   PubMed Web of Science ®Google Scholar
• Wang L, Cheng W, Zhang Z. 2017. Respiratory syncytial virus infection accelerates lung fibrosis through the unfolded protein response in a bleomycin-induced pulmonary fibrosis animal model. Mol Med Rep. 16(1):310–316. doi: 10.3892/mmr.2017.6558.
   PubMed Web of Science ®Google Scholar
• Watanabe Y, Bowden TA, Wilson IA, Crispin M. 2019. Exploitation of glycosylation in enveloped virus pathobiology. Biochim Biophys Acta Gen Subj. 1863(10):1480–1497. doi: 10.1016/j.bbagen.2019.05.012.
   PubMed Web of Science ®Google Scholar
• Wong MY, Chen K, Antonopoulos A, Kasper BT, Dewal MB, Taylor RJ, Whittaker CA, Hein PP, Dell A, Genereux JC, et al. 2018. XBP1s activation can globally remodel N-glycan structure distribution patterns. Proc Natl Acad Sci U S A. 115(43):E10089–E10098. doi: 10.1073/pnas.1805425115.
   PubMed Web of Science ®Google Scholar
• Wu C-Y, Cheng C-W, Kung C-C, Liao K-S, Jan J-T, Ma C, Wong C-H. 2022. Glycosite-deleted mRNA of SARS-CoV-2 spike protein as a broad-spectrum vaccine. Proc Natl Acad Sci U S A. 119(9):e2119995119. doi: 10.1073/pnas.2119995119.
   PubMed Web of Science ®Google Scholar
• Xu X, Gupta S, Hu W, McGrath BC, Cavener DR. 2011. Hyperthermia induces the ER stress pathway. PLoS One. 6(8):e23740. doi: 10.1371/journal.pone.0023740.
   PubMed Web of Science ®Google Scholar
• Xue M, Feng L. 2021. The role of unfolded protein response in coronavirus infection and its implications for drug design. Front Microbiol. 12:808593. doi: 10.3389/fmicb.2021.808593.
   PubMed Web of Science ®Google Scholar
• Yan W, Frank CL, Korth MJ, Sopher BL, Novoa I, Ron D, Katze MG. 2002. Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc Natl Acad Sci U S A. 99(25):15920–15925. doi: 10.1073/pnas.252341799.
   PubMed Web of Science ®Google Scholar
• Ye Z, Wong CK, Li P, Xie Y. 2008. A SARS-CoV protein, ORF-6, induces caspase-3 mediated, ER stress and JNK-dependent apoptosis. Biochim Biophys Acta. 1780(12):1383–1387. doi: 10.1016/j.bbagen.2008.07.009.
   PubMed Web of Science ®Google Scholar
• Yin Y, Yu S, Sun Y, Qin T, Chen S, Ding C, Peng D, Liu X. 2020. Glycosylation deletion of hemagglutinin head in the H5 subtype avian influenza virus enhances its virulence in mammals by inducing endoplasmic reticulum stress. Transbound Emerg Dis. 67(4):1492–1506. doi: 10.1111/tbed.13481.
   PubMed Web of Science ®Google Scholar
• York Ian A, Stevens J, Alymova IV. 2019. Influenza virus N-linked glycosylation and innate immunity. Biosci Rep. 39(1):BSR20171505. doi: 10.1042/bsr20171505.
   PubMedGoogle Scholar
• Zamarin D, Ortigoza MB, Palese P. 2006. Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice. J Virol. 80(16):7976–7983. doi: 10.1128/jvi.00415-06.
   PubMed Web of Science ®Google Scholar
• Zhang J, Ejikemeuwa A, Gerzanich V, Nasr M, Tang Q, Simard JM, Zhao RY. 2022. Understanding the role of SARS-CoV-2 ORF3a in viral pathogenesis and COVID-19. Front Microbiol. 13:854567. doi: 10.3389/fmicb.2022.854567.
   PubMed Web of Science ®Google Scholar
• Zhang K, Kaufman RJ. 2008. From endoplasmic-reticulum stress to the inflammatory response. Nature. 454(7203):455–462. doi: 10.1038/nature07203.
   PubMed Web of Science ®Google Scholar
• Zhang L, Zhang C, Wang A. 2016. Divergence and conservation of the major UPR branch IRE1-bZIP signaling pathway across eukaryotes. Sci Rep. 6(1):27362. doi: 10.1038/srep27362.
   PubMedGoogle Scholar
• Zhang X, Chen S, Jiang Y, Huang K, Huang J, Yang D, Zhu J, Zhu Y, Shi S, Peng D, et al. 2015. Hemagglutinin glycosylation modulates the pathogenicity and antigenicity of the H5N1 avian influenza virus. Vet Microbiol. 175(2-4):244–256. doi: 10.1016/j.vetmic.2014.12.011.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Zhu J, Li Y, Bradley KC, Cao J, Chen H, Jin M, Zhou H. 2013. Glycosylation on hemagglutinin affects the virulence and pathogenicity of pandemic H1N1/2009 influenza A virus in mice. PLoS One. 8(4):e61397. doi: 10.1371/journal.pone.0061397.
   PubMed Web of Science ®Google Scholar
• Zhu Z, Lian X, Su X, Wu W, Marraro GA, Zeng Y. 2020. From SARS and MERS to COVID-19: a brief summary and comparison of severe acute respiratory infections caused by three highly pathogenic human coronaviruses. Respir Res. 21(1):224. doi: 10.1186/s12931-020-01479-w.
   PubMed Web of Science ®Google Scholar
• Zimmer G, Trotz I, Herrler G. 2001. N-glycans of F protein differentially affect fusion activity of human respiratory syncytial virus. J Virol. 75(10):4744–4751. doi: 10.1128/JVI.75.10.4744-4751.2001.
   PubMed Web of Science ®Google Scholar