ACE2 and Innate Immunity in the Regulation of SARS-CoV-2-Induced Acute Lung Injury: A Review
Abstract
:1. Introduction
2. ACE2 and COVID-19
2.1. The Biological Function of ACE2
2.2. ACE2 and SARS-CoV-2 in ALI
3. The Role of ACE2 in Innate Immune-Related Cells during SARS-CoV-2 Infection
4. ACE2, SARS-CoV-2, and Innate Immune Pathways
4.1. TLRs Pathway
4.2. RIG-I/MDA5 Pathway
4.3. cGAS/STING Pathway
4.4. NLRs Signaling Pathway
5. The Potential Therapeutic Role of ACE2 in COVID-19
5.1. Chloroquine
5.2. ACEI or ARBs
5.3. Recombinant ACE2
5.4. Vitamin D
Drug | Major Outcome(s) Relates to ACE2 and SARS-CoV-2 | References |
---|---|---|
Chloroquine | Chloroquine inhibited the binding of SARS-CoV-2 to ACE2, reducing the infection of the host cell by the virus. However, an increase in overall mortality was found in patients treated with chloroquine. | Ortiz MEetal., 2020 [173] Devaux et al., 2020 [174] Joseph et al., 2020 [182] |
ACEI or ARBs | ACEI or ARBs inhibited the ACE/Ang/AT1R pathway to reduce inflammatory response and alleviate ARDS. | Neyrinck et al., 2009 [184] Melissa et al., 2021 [185] Yisireyili M et al., 2018 [186] |
rhACE2 | rhACE2 could bind to the spike protein by competing with ACE2 on the cell membrane surface, which on the one hand, inhibited the virus from infecting cells, on the other hand, rhACE2 could activate ACE2-Ang (1-7)-MasR pathway, reducing lung inflammation, and alleviating lung injury or ARDS. | Gheblawi et al., 2020 [40] Guzik et al., 2020 [192] Hoepel et al., 2021 [196] |
Vitamin D | Vitamin D reduced oxidative stress and inflammation, enhancing innate immunity, and downregulating the expression of ACE2 to reduce the severity of SARS-CoV-2 infection. | Mendonca et al., 2020 [205] |
6. Conclusions Remarks and Future Perspectives
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
Abbreviations
ACE2 | Angiotensin-converting enzyme 2 |
ARBs | Angiotensin receptor blockers |
ALI | Acute lung injury |
AT1R | Angiotensin type 1 receptor |
AT2R | Angiotensin 2 receptor |
ACEI | Angiotensin-converting enzyme inhibitor |
Ang II | Angiotensin II |
COVID-19 | Coronavirus disease |
cGAS | Cyclic guanosine phosphate adenosine phosphate synthase |
cGAMP | Cyclic guanosine monophosphate adenosine monophosphate |
DCs | Dendritic cells |
IRF3 | Interferon regulatory factor 3 |
MDA5 | Melanoma differentiation associated gene 5 |
MAVS | Mitochondrial antiviral-signaling protein |
MasR | Mas receptor |
MyD88 | Myeloid cell differentiation factor 88 |
NLRs | Nucleotide-binding oligomerization domain-like receptors |
NLRP3 | NOD-like receptor family pyrin domain containing 3 |
PRRs | Pattern recognition receptors |
RAS | Renin-angiotensin system |
rhACE2 | Recombinant human angiotensin converting enzyme 2 |
RIG-I | Retinoic acid-inducible gene I |
SARS-CoV-2 | Severe Acute Respiratory Syndrome Coronavirus 2 |
STING | Stimulator of interferon genes |
TLRs | Toll-like receptors |
References
- Xu, M.; Wang, D.; Wang, H.; Zhang, X.; Liang, T.; Dai, J.; Li, M.; Zhang, J.; Zhang, K.; Xu, D.; et al. COVID-19 diagnostic testing: Technology perspective. Clin. Transl. Med. 2020, 10, e158. [Google Scholar] [CrossRef]
- Zhang, Z.; Wang, X.; Wei, X.; Zheng, S.W.; Lenhart, B.J.; Xu, P.; Li, J.; Pan, J.; Albrecht, H.; Liu, C. Multiplex quantitative detection of SARS-CoV-2 specific IgG and IgM antibodies based on DNA-assisted nanopore sensing. Biosens. Bioelectron. 2021, 181, 113134. [Google Scholar] [CrossRef] [PubMed]
- Kola, L.; Kohrt, B.A.; Hanlon, C.; Naslund, J.A.; Sikander, S.; Balaji, M.; Benjet, C.; Cheung, E.Y.L.; Eaton, J.; Gonsalves, P.; et al. COVID-19 mental health impact and responses in low-income and middle-income countries: Reimagining global mental health. Lancet Psychiatry 2021, 8, 535–550. [Google Scholar] [CrossRef]
- Huang, C.; Wang, Y.; Li, X.; Ren, L.; Zhao, J.; Hu, Y.; Zhang, L.; Fan, G.; Xu, J.; Gu, X.; et al. Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China. Lancet 2020, 395, 497–506. [Google Scholar] [CrossRef] [Green Version]
- Zhu, N.; Zhang, D.; Wang, W.; Li, X.; Yang, B.; Song, J.; Zhao, X.; Huang, B.; Shi, W.; Lu, R.; et al. A Novel Coronavirus from Patients with Pneumonia in China, 2019. N. Engl. J. Med. 2020, 382, 727–733. [Google Scholar] [CrossRef]
- Salter, A.; Fox, R.J.; Newsome, S.D.; Halper, J.; Li, D.K.B.; Kanellis, P.; Costello, K.; Bebo, B.; Rammohan, K.; Cutter, G.R.; et al. Outcomes and Risk Factors Associated with SARS-CoV-2 Infection in a North American Registry of Patients with Multiple Sclerosis. JAMA Neurol. 2021, 78, 699–708. [Google Scholar] [CrossRef] [PubMed]
- Ji, L.; Cao, C.; Gao, Y.; Zhang, W.; Xie, Y.; Duan, Y.; Kong, S.; You, M.; Ma, R.; Jiang, L.; et al. Prognostic value of bedside lung ultrasound score in patients with COVID-19. Crit. Care 2020, 24, 700. [Google Scholar] [CrossRef]
- Chan, S.W. Current and Future Direct-Acting Antivirals against COVID-19. Front. Microbiol. 2020, 11, 587944. [Google Scholar] [CrossRef]
- Xiao, N.; Nie, M.; Pang, H.; Wang, B.; Hu, J.; Meng, X.; Li, K.; Ran, X.; Long, Q.; Deng, H.; et al. Integrated cytokine and metabolite analysis reveals immunometabolic reprogramming in COVID-19 patients with therapeutic implications. Nat. Commun. 2021, 12, 1618. [Google Scholar] [CrossRef]
- Rodda, L.B.; Netland, J.; Shehata, L.; Pruner, K.B.; Morawski, P.A.; Thouvenel, C.D.; Takehara, K.K.; Eggenberger, J.; Hemann, E.A.; Waterman, H.R.; et al. Functional SARS-CoV-2-Specific Immune Memory Persists after Mild COVID-19. Cell 2021, 184, 169–183.e117. [Google Scholar] [CrossRef]
- Livanos, A.E.; Jha, D.; Cossarini, F.; Gonzalez-Reiche, A.S.; Tokuyama, M.; Aydillo, T.; Parigi, T.L.; Ladinsky, M.S.; Ramos, I.; Dunleavy, K.; et al. Intestinal Host Response to SARS-CoV-2 Infection and COVID-19 Outcomes in Patients with Gastrointestinal Symptoms. Gastroenterology 2021, 60, 2435–2450.e34. [Google Scholar] [CrossRef]
- Vella, L.A.; Giles, J.R.; Baxter, A.E.; Oldridge, D.A.; Diorio, C.; Kuri-Cervantes, L.; Alanio, C.; Pampena, M.B.; Wu, J.E.; Chen, Z.; et al. Deep immune profiling of MIS-C demonstrates marked but transient immune activation compared to adult and pediatric COVID-19. Sci. Immunol. 2021, 6, eabf7570. [Google Scholar] [CrossRef]
- Kai, H.; Kai, M. Interactions of coronaviruses with ACE2, angiotensin II, and RAS inhibitors-lessons from available evidence and insights into COVID-19. Hypertens. Res. 2020, 43, 648–654. [Google Scholar] [CrossRef] [PubMed]
- Pabalan, N.; Tharabenjasin, P.; Suntornsaratoon, P.; Jarjanazi, H.; Muanprasat, C. Ethnic and age-specific acute lung injury/acute respiratory distress syndrome risk associated with angiotensin-converting enzyme insertion/deletion polymorphisms, implications for COVID-19: A meta-analysis. Infect. Genet. Evol. 2021, 88, 104682. [Google Scholar] [CrossRef]
- Cruces, P.; Diaz, F.; Puga, A.; Erranz, B.; Donoso, A.; Carvajal, C.; Wilhelm, J.; Repetto, G.M. Angiotensin-converting enzyme insertion/deletion polymorphism is associated with severe hypoxemia in pediatric ARDS. Intensive Care Med. 2012, 38, 113–119. [Google Scholar] [CrossRef] [PubMed]
- Montalvan, V.; Lee, J.; Bueso, T.; De Toledo, J.; Rivas, K. Neurological manifestations of COVID-19 and other coronavirus infections: A systematic review. Clin. Neurol. Neurosurg. 2020, 194, 105921. [Google Scholar] [CrossRef]
- Datta, P.K.; Liu, F.; Fischer, T.; Rappaport, J.; Qin, X. SARS-CoV-2 pandemic and research gaps: Understanding SARS-CoV-2 interaction with the ACE2 receptor and implications for therapy. Theranostics 2020, 10, 7448–7464. [Google Scholar] [CrossRef] [PubMed]
- Cozier, G.E.; Lubbe, L.; Sturrock, E.D.; Acharya, K.R. Angiotensin-converting enzyme open for business: Structural insights into the subdomain dynamics. FEBS J. 2021, 288, 2238–2256. [Google Scholar] [CrossRef]
- Davidson, A.M.; Wysocki, J.; Batlle, D. Interaction of SARS-CoV-2 and Other Coronavirus with ACE (Angiotensin-Converting Enzyme)-2 as Their Main Receptor: Therapeutic Implications. Hypertension 2020, 76, 1339–1349. [Google Scholar] [CrossRef]
- Riordan, J.F. Angiotensin-I-converting enzyme and its relatives. Genome Biol. 2003, 4, 225. [Google Scholar] [CrossRef] [Green Version]
- Lieb, W.; Graf, J.; Gotz, A.; Konig, I.R.; Mayer, B.; Fischer, M.; Stritzke, J.; Hengstenberg, C.; Holmer, S.R.; Doring, A.; et al. Association of angiotensin-converting enzyme 2 (ACE2) gene polymorphisms with parameters of left ventricular hypertrophy in men. Results of the MONICA Augsburg echocardiographic substudy. J. Mol. Med. 2006, 84, 88–96. [Google Scholar] [CrossRef] [PubMed]
- Donoghue, M.; Hsieh, F.; Baronas, E.; Godbout, K.; Gosselin, M.; Stagliano, N.; Donovan, M.; Woolf, B.; Robison, K.; Jeyaseelan, R.; et al. A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ. Res. 2000, 87, e1–e9. [Google Scholar] [CrossRef] [PubMed]
- Imai, Y.; Kuba, K.; Rao, S.; Huan, Y.; Guo, F.; Guan, B.; Yang, P.; Sarao, R.; Wada, T.; Leong-Poi, H.; et al. Angiotensin-converting enzyme 2 protects from severe acute lung failure. Nature 2005, 436, 112–116. [Google Scholar] [CrossRef]
- Ferrario, C.M.; Chappell, M.C. Novel angiotensin peptides. Cell Mol. Life Sci. 2004, 61, 2720–2727. [Google Scholar] [CrossRef] [PubMed]
- Li, X.C.; Zhu, D.; Zheng, X.; Zhang, J.; Zhuo, J.L. Intratubular and intracellular renin-angiotensin system in the kidney: A unifying perspective in blood pressure control. Clin. Sci. 2018, 132, 1383–1401. [Google Scholar] [CrossRef] [PubMed]
- Prieto, I.; Villarejo, A.B.; Segarra, A.B.; Banegas, I.; Wangensteen, R.; Martinez-Canamero, M.; de Gasparo, M.; Vives, F.; Ramirez-Sanchez, M. Brain, heart and kidney correlate for the control of blood pressure and water balance: Role of angiotensinases. Neuroendocrinology 2014, 100, 198–208. [Google Scholar] [CrossRef] [PubMed]
- Steckelings, U.M.; Sumners, C. Correcting the imbalanced protective RAS in COVID-19 with angiotensin AT2-receptor agonists. Clin. Sci. 2020, 134, 2987–3006. [Google Scholar] [CrossRef]
- Pedrosa, M.A.; Valenzuela, R.; Garrido-Gil, P.; Labandeira, C.M.; Navarro, G.; Franco, R.; Labandeira-Garcia, J.L.; Rodriguez-Perez, A.I. Experimental data using candesartan and captopril indicate no double-edged sword effect in COVID-19. Clin. Sci. 2021, 135, 465–481. [Google Scholar] [CrossRef]
- Ribeiro, V.T.; Cordeiro, T.M.E.; Filha, R.D.S.; Perez, L.G.; Caramelli, P.; Teixeira, A.L.; de Souza, L.C.; Simoes, E.S.A.C. Circulating Angiotensin-(1-7) Is Reduced in Alzheimer’s Disease Patients and Correlates with White Matter Abnormalities: Results From a Pilot Study. Front. Neurosci. 2021, 15, 636754. [Google Scholar] [CrossRef]
- Hrenak, J.; Simko, F. Renin-Angiotensin System: An Important Player in the Pathogenesis of Acute Respiratory Distress Syndrome. Int. J. Mol. Sci. 2020, 21, 8038. [Google Scholar] [CrossRef]
- Gnanenthiran, S.R.; Borghi, C.; Burger, D.; Charchar, F.; Poulter, N.R.; Schlaich, M.P.; Steckelings, U.M.; Stergiou, G.; Tomaszewski, M.; Unger, T.; et al. Prospective meta-analysis protocol on randomised trials of renin-angiotensin system inhibitors in patients with COVID-19: An initiative of the International Society of Hypertension. BMJ Open 2021, 11, e043625. [Google Scholar] [CrossRef] [PubMed]
- Passos-Silva, D.G.; Verano-Braga, T.; Santos, R.A. Angiotensin-(1-7): Beyond the cardio-renal actions. Clin. Sci. 2013, 124, 443–456. [Google Scholar] [CrossRef] [Green Version]
- Verma, A.; Shan, Z.; Lei, B.; Yuan, L.; Liu, X.; Nakagawa, T.; Grant, M.B.; Lewin, A.S.; Hauswirth, W.W.; Raizada, M.K.; et al. ACE2 and Ang-(1-7) confer protection against development of diabetic retinopathy. Mol. Ther. 2012, 20, 28–36. [Google Scholar] [CrossRef] [Green Version]
- Trougakos, I.P.; Stamatelopoulos, K.; Terpos, E.; Tsitsilonis, O.E.; Aivalioti, E.; Paraskevis, D.; Kastritis, E.; Pavlakis, G.N.; Dimopoulos, M.A. Insights to SARS-CoV-2 life cycle, pathophysiology, and rationalized treatments that target COVID-19 clinical complications. J. Biomed. Sci. 2021, 28, 9. [Google Scholar] [CrossRef] [PubMed]
- Chen, I.C.; Lin, J.Y.; Liu, Y.C.; Chai, C.Y.; Yeh, J.L.; Hsu, J.H.; Wu, B.N.; Dai, Z.K. Angiotensin-Converting Enzyme 2 Activator Ameliorates Severe Pulmonary Hypertension in a Rat Model of Left Pneumonectomy Combined with VEGF Inhibition. Front. Med. 2021, 8, 619133. [Google Scholar] [CrossRef] [PubMed]
- Shim, K.Y.; Eom, Y.W.; Kim, M.Y.; Kang, S.H.; Baik, S.K. Role of the renin-angiotensin system in hepatic fibrosis and portal hypertension. Korean J. Intern. Med. 2018, 33, 453–461. [Google Scholar] [CrossRef] [Green Version]
- Fliser, D.; Buchholz, K.; Haller, H.; EUropean Trial on Olmesartan and Pravastatin in Inflammation and Atherosclerosis (EUTOPIA) Investigators. Antiinflammatory effects of angiotensin II subtype 1 receptor blockade in hypertensive patients with microinflammation. Circulation 2004, 110, 1103–1107. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Khanna, P.; Soh, H.J.; Chen, C.H.; Saxena, R.; Amin, S.; Naughton, M.; Joslin, P.N.; Moore, A.; Bakouny, Z.; O’Callaghan, C.; et al. ACE2 abrogates tumor resistance to VEGFR inhibitors suggesting angiotensin-(1-7) as a therapy for clear cell renal cell carcinoma. Sci. Transl. Med. 2021, 13, eabc0170. [Google Scholar] [CrossRef] [PubMed]
- Keidar, S.; Kaplan, M.; Gamliel-Lazarovich, A. ACE2 of the heart: From angiotensin I to angiotensin (1-7). Cardiovasc. Res. 2007, 73, 463–469. [Google Scholar] [CrossRef]
- Gheblawi, M.; Wang, K.; Viveiros, A.; Nguyen, Q.; Zhong, J.C.; Turner, A.J.; Raizada, M.K.; Grant, M.B.; Oudit, G.Y. Angiotensin-Converting Enzyme 2: SARS-CoV-2 Receptor and Regulator of the Renin-Angiotensin System: Celebrating the 20th Anniversary of the Discovery of ACE2. Circ. Res. 2020, 126, 1456–1474. [Google Scholar] [CrossRef]
- Knight, A.C.; Montgomery, S.A.; Fletcher, C.A.; Baxter, V.K. Mouse Models for the Study of SARS-CoV-2 Infection. Comp. Med. 2021. [Google Scholar] [CrossRef] [PubMed]
- Zhou, X.; Ma, F.; Xie, J.; Yuan, M.; Li, Y.; Shaabani, N.; Zhao, F.; Huang, D.; Wu, N.C.; Lee, C.D.; et al. Diverse immunoglobulin gene usage and convergent epitope targeting in neutralizing antibody responses to SARS-CoV-2. Cell Rep. 2021, 35, 109109. [Google Scholar] [CrossRef] [PubMed]
- South, A.M.; Shaltout, H.A.; Washburn, L.K.; Hendricks, A.S.; Diz, D.I.; Chappell, M.C. Fetal programming and the angiotensin-(1-7) axis: A review of the experimental and clinical data. Clin. Sci. 2019, 133, 55–74. [Google Scholar] [CrossRef] [PubMed]
- Kuba, K.; Imai, Y.; Rao, S.; Gao, H.; Guo, F.; Guan, B.; Huan, Y.; Yang, P.; Zhang, Y.; Deng, W.; et al. A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus-induced lung injury. Nat. Med. 2005, 11, 875–879. [Google Scholar] [CrossRef]
- Kuba, K.; Imai, Y.; Rao, S.; Jiang, C.; Penninger, J.M. Lessons from SARS: Control of acute lung failure by the SARS receptor ACE2. J. Mol. Med. 2006, 84, 814–820. [Google Scholar] [CrossRef] [PubMed]
- Wosten-van Asperen, R.M.; Lutter, R.; Specht, P.A.; Moll, G.N.; van Woensel, J.B.; van der Loos, C.M.; van Goor, H.; Kamilic, J.; Florquin, S.; Bos, A.P. Acute respiratory distress syndrome leads to reduced ratio of ACE/ACE2 activities and is prevented by angiotensin-(1-7) or an angiotensin II receptor antagonist. J. Pathol. 2011, 225, 618–627. [Google Scholar] [CrossRef]
- Huentelman, M.J.; Zubcevic, J.; Hernandez Prada, J.A.; Xiao, X.; Dimitrov, D.S.; Raizada, M.K.; Ostrov, D.A. Structure-based discovery of a novel angiotensin-converting enzyme 2 inhibitor. Hypertension 2004, 44, 903–906. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Khan, A.; Benthin, C.; Zeno, B.; Albertson, T.E.; Boyd, J.; Christie, J.D.; Hall, R.; Poirier, G.; Ronco, J.J.; Tidswell, M.; et al. A pilot clinical trial of recombinant human angiotensin-converting enzyme 2 in acute respiratory distress syndrome. Crit. Care 2017, 21, 234. [Google Scholar] [CrossRef] [Green Version]
- Chen, Y.; Qu, L.; Li, Y.; Chen, C.; He, W.; Shen, L.; Zhang, R. Glycyrrhizic Acid Alleviates Lipopolysaccharide (LPS)-Induced Acute Lung Injury by Regulating Angiotensin-Converting Enzyme-2 (ACE2) and Caveolin-1 Signaling Pathway. Inflammation 2021, 1–14. [Google Scholar] [CrossRef]
- Huang, K.; Zhang, P.; Zhang, Z.; Youn, J.Y.; Wang, C.; Zhang, H.; Cai, H. Traditional Chinese Medicine (TCM) in the treatment of COVID-19 and other viral infections: Efficacies and mechanisms. Pharmacol. Ther. 2021, 225, 107843. [Google Scholar] [CrossRef] [PubMed]
- Meydan, C.; Madrer, N.; Soreq, H. The Neat Dance of COVID-19: NEAT1, DANCR, and Co-Modulated Cholinergic RNAs Link to Inflammation. Front. Immunol. 2020, 11, 590870. [Google Scholar] [CrossRef] [PubMed]
- Gao, Y.L.; Du, Y.; Zhang, C.; Cheng, C.; Yang, H.Y.; Jin, Y.F.; Duan, G.C.; Chen, S.Y. Role of Renin-Angiotensin System in Acute Lung Injury Caused by Viral Infection. Infect. Drug Resist. 2020, 13, 3715–3725. [Google Scholar] [CrossRef]
- Gerard, L.; Lecocq, M.; Bouzin, C.; Hoton, D.; Schmit, G.; Pereira, J.P.; Montiel, V.; Plante-Bordeneuve, T.; Laterre, P.F.; Pilette, C. Increased Angiotensin-Converting Enzyme 2 and Loss of Alveolar Type II Cells in COVID-19 Related ARDS. Am. J. Respir. Crit. Care Med. 2021. [Google Scholar] [CrossRef]
- Asaka, M.N.; Utsumi, D.; Kamada, H.; Nagata, S.; Nakachi, Y.; Yamaguchi, T.; Kawaoka, Y.; Kuba, K.; Yasutomi, Y. Highly susceptible SARS-CoV-2 model in CAG promoter-driven hACE2-transgenic mice. JCI Insight 2021, 6, e152529. [Google Scholar] [CrossRef]
- Herman-Edelstein, M.; Guetta, T.; Barnea, A.; Waldman, M.; Ben-Dor, N.; Barak, Y.; Kornowski, R.; Arad, M.; Hochhauser, E.; Aravot, D. Expression of the SARS-CoV-2 receptorACE2 in human heart is associated with uncontrolled diabetes, obesity, and activation of the renin angiotensin system. Cardiovasc. Diabetol. 2021, 20, 90. [Google Scholar] [CrossRef] [PubMed]
- Savoia, C.; Volpe, M.; Kreutz, R. Hypertension, a Moving Target in COVID-19: Current Views and Perspectives. Circ. Res. 2021, 128, 1062–1079. [Google Scholar] [CrossRef] [PubMed]
- Rico-Mesa, J.S.; White, A.; Anderson, A.S. Outcomes in Patients with COVID-19 Infection Taking ACEI/ARB. Curr. Cardiol. Rep. 2020, 22, 31. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Chu, C.; Zeng, S.; Hasan, A.A.; Hocher, C.F.; Kramer, B.K.; Hocher, B. Comparison of infection risks and clinical outcomes in patients with and without SARS-CoV-2 lung infection under renin-angiotensin-aldosterone system blockade: Systematic review and meta-analysis. Br. J. Clin. Pharmacol. 2020, 87, 2475–2492. [Google Scholar] [CrossRef]
- Lee, H.W.; Yoon, C.H.; Jang, E.J.; Lee, C.H. Renin-angiotensin system blocker and outcomes of COVID-19: A systematic review and meta-analysis. Thorax 2021, 76, 479–486. [Google Scholar] [CrossRef]
- Xu, J.; Teng, Y.; Shang, L.; Gu, X.; Fan, G.; Chen, Y.; Tian, R.; Zhang, S.; Cao, B. The Effect of Prior ACEI/ARB Treatment on COVID-19 Susceptibility and Outcome: A Systematic Review and Meta-Analysis. Clin. Infect. Dis. 2020, 72, e901–e913. [Google Scholar] [CrossRef] [PubMed]
- Volpe, M.; Patrono, C. A randomized trial supports the recommendation to continue treatment with ACEi or ARBs during hospitalization for COVID-19. Eur. Heart J. 2021, 42, 1061–1062. [Google Scholar] [CrossRef] [PubMed]
- Nieto-Torres, J.L.; Verdia-Baguena, C.; Jimenez-Guardeno, J.M.; Regla-Nava, J.A.; Castano-Rodriguez, C.; Fernandez-Delgado, R.; Torres, J.; Aguilella, V.M.; Enjuanes, L. Severe acute respiratory syndrome coronavirus E protein transports calcium ions and activates the NLRP3 inflammasome. Virology 2015, 485, 330–339. [Google Scholar] [CrossRef] [Green Version]
- Jimenez-Guardeno, J.M.; Nieto-Torres, J.L.; DeDiego, M.L.; Regla-Nava, J.A.; Fernandez-Delgado, R.; Castano-Rodriguez, C.; Enjuanes, L. The PDZ-binding motif of severe acute respiratory syndrome coronavirus envelope protein is a determinant of viral pathogenesis. PLoS Pathog 2014, 10, e1004320. [Google Scholar] [CrossRef] [Green Version]
- Teoh, K.T.; Siu, Y.L.; Chan, W.L.; Schluter, M.A.; Liu, C.J.; Peiris, J.S.; Bruzzone, R.; Margolis, B.; Nal, B. The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis. Mol. Biol. Cell 2010, 21, 3838–3852. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Muus, C.; Luecken, M.D.; Eraslan, G.; Sikkema, L.; Waghray, A.; Heimberg, G.; Kobayashi, Y.; Vaishnav, E.D.; Subramanian, A.; Smillie, C.; et al. Single-cell meta-analysis of SARS-CoV-2 entry genes across tissues and demographics. Nat. Med. 2021, 27, 546–559. [Google Scholar] [CrossRef] [PubMed]
- Wang, S.; Qiu, Z.; Hou, Y.; Deng, X.; Xu, W.; Zheng, T.; Wu, P.; Xie, S.; Bian, W.; Zhang, C.; et al. AXL is a candidate receptor for SARS-CoV-2 that promotes infection of pulmonary and bronchial epithelial cells. Cell Res. 2021, 31, 126–140. [Google Scholar] [CrossRef]
- McCracken, I.R.; Saginc, G.; He, L.; Huseynov, A.; Daniels, A.; Fletcher, S.; Peghaire, C.; Kalna, V.; Andaloussi-Mae, M.; Muhl, L.; et al. Lack of Evidence of Angiotensin-Converting Enzyme 2 Expression and Replicative Infection by SARS-CoV-2 in Human Endothelial Cells. Circulation 2021, 143, 865–868. [Google Scholar] [CrossRef]
- Ramassamy, J.L.; Tortevoye, P.; Ntab, B.; Seve, B.; Carles, G.; Gaquiere, D.; Madec, Y.; Fontanet, A.; Gessain, A. Adult T-cell leukemia/lymphoma incidence rate in French Guiana: A prospective cohort of women infected with HTLV-1. Blood Adv. 2020, 4, 2044–2048. [Google Scholar] [CrossRef]
- Ma, D.; Liu, S.; Hu, L.; He, Q.; Shi, W.; Yan, D.; Cao, Y.; Zhang, G.; Wang, Z.; Wu, J.; et al. Single-cell RNA sequencing identify SDCBP in ACE2-positive bronchial epithelial cells negatively correlates with COVID-19 severity. J. Cell Mol. Med. 2021, 25, 7001–7012. [Google Scholar] [CrossRef]
- Dikshith, T.S.; Raizada, R.B.; Kumar, S.N.; Srivastava, M.K.; Kaushal, R.A.; Singh, R.P.; Gupta, K.P. Effect of repeated dermal application of endosulfan to rats. Vet. Hum. Toxicol. 1988, 30, 219–224. [Google Scholar]
- Aboudounya, M.M.; Heads, R.J. COVID-19 and Toll-Like Receptor 4 (TLR4): SARS-CoV-2 May Bind and Activate TLR4 to Increase ACE2 Expression, Facilitating Entry and Causing Hyperinflammation. Mediat. Inflamm. 2021, 2021, 8874339. [Google Scholar] [CrossRef]
- Yang, X.; Yu, Y.; Xu, J.; Shu, H.; Xia, J.; Liu, H.; Wu, Y.; Zhang, L.; Yu, Z.; Fang, M.; et al. Clinical course and outcomes of critically ill patients with SARS-CoV-2 pneumonia in Wuhan, China: A single-centered, retrospective, observational study. Lancet Respir. Med. 2020, 8, 475–481. [Google Scholar] [CrossRef] [Green Version]
- Obukhov, A.G.; Stevens, B.R.; Prasad, R.; Li Calzi, S.; Boulton, M.E.; Raizada, M.K.; Oudit, G.Y.; Grant, M.B. SARS-CoV-2 Infections and ACE2: Clinical Outcomes Linked with Increased Morbidity and Mortality in Individuals with Diabetes. Diabetes 2020, 69, 1875–1886. [Google Scholar] [CrossRef] [PubMed]
- Zhang, X.; Zheng, J.; Yan, Y.; Ruan, Z.; Su, Y.; Wang, J.; Huang, H.; Zhang, Y.; Wang, W.; Gao, J.; et al. Angiotensin-converting enzyme 2 regulates autophagy in acute lung injury through AMPK/mTOR signaling. Arch. Biochem. Biophys. 2019, 672, 108061. [Google Scholar] [CrossRef] [PubMed]
- Caci, G.; Albini, A.; Malerba, M.; Noonan, D.M.; Pochetti, P.; Polosa, R. COVID-19 and Obesity: Dangerous Liaisons. J. Clin. Med. 2020, 9, 2511. [Google Scholar] [CrossRef] [PubMed]
- De Oliveira, A.P.; Lopes, A.L.F.; Pacheco, G.; de Sa Guimaraes Noleto, I.R.; Nicolau, L.A.D.; Medeiros, J.V.R. Premises among SARS-CoV-2, dysbiosis and diarrhea: Walking through the ACE2/mTOR/autophagy route. Med. Hypotheses 2020, 144, 110243. [Google Scholar] [CrossRef]
- Li, Y.; Cao, Y.; Zeng, Z.; Liang, M.; Xue, Y.; Xi, C.; Zhou, M.; Jiang, W. Angiotensin-converting enzyme 2/angiotensin-(1-7)/Mas axis prevents lipopolysaccharide-induced apoptosis of pulmonary microvascular endothelial cells by inhibiting JNK/NF-kappaB pathways. Sci. Rep. 2015, 5, 8209. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Uhal, B.D.; Li, X.; Xue, A.; Gao, X.; Abdul-Hafez, A. Regulation of alveolar epithelial cell survival by the ACE-2/angiotensin 1-7/Mas axis. Am. J. Physiol. Lung Cell Mol. Physiol. 2011, 301, L269–L274. [Google Scholar] [CrossRef] [Green Version]
- Hasan, H.F.; Elgazzar, E.M.; Mostafa, D.M. Diminazene aceturate extenuate the renal deleterious consequences of angiotensin-II induced by gamma-irradiation through boosting ACE2 signaling cascade. Life Sci. 2020, 253, 117749. [Google Scholar] [CrossRef]
- Wang, J.; Kaplan, N.; Wysocki, J.; Yang, W.; Lu, K.; Peng, H.; Batlle, D.; Lavker, R.M. The ACE2-deficient mouse: A model for a cytokine storm-driven inflammation. FASEB J. 2020, 34, 10505–10515. [Google Scholar] [CrossRef]
- Shen, L.; Mo, H.; Cai, L.; Kong, T.; Zheng, W.; Ye, J.; Qi, J.; Xiao, Z. Losartan prevents sepsis-induced acute lung injury and decreases activation of nuclear factor kappaB and mitogen-activated protein kinases. Shock 2009, 31, 500–506. [Google Scholar] [CrossRef]
- Sharif-Askari, N.S.; Sharif-Askari, F.S.; Mdkhana, B.; Hussain Alsayed, H.A.; Alsafar, H.; Alrais, Z.F.; Hamid, Q.; Halwani, R. Upregulation of oxidative stress gene markers during SARS-CoV-2 viral infection. Free Radic. Biol. Med. 2021, 172, 688–698. [Google Scholar] [CrossRef] [PubMed]
- Chi, Y.; Ge, Y.; Wu, B.; Zhang, W.; Wu, T.; Wen, T.; Liu, J.; Guo, X.; Huang, C.; Jiao, Y.; et al. Serum Cytokine and Chemokine Profile in Relation to the Severity of Coronavirus Disease 2019 in China. J. Infect. Dis. 2020, 222, 746–754. [Google Scholar] [CrossRef] [PubMed]
- Zhang, W.; Dai, H.; Lin, F.; Zhao, C.; Wang, X.; Zhang, S.; Ge, W.; Pei, S.; Pan, L. Ly-6C(high) inflammatory-monocyte recruitment is regulated by p38 MAPK/MCP-1 activation and promotes ventilator-induced lung injury. Int. Immunopharmacol. 2020, 78, 106015. [Google Scholar] [CrossRef]
- Robinson, D.P.; Hall, O.J.; Nilles, T.L.; Bream, J.H.; Klein, S.L. 17beta-estradiol protects females against influenza by recruiting neutrophils and increasing virus-specific CD8 T cell responses in the lungs. J. Virol. 2014, 88, 4711–4720. [Google Scholar] [CrossRef] [Green Version]
- Li, S.; Zhang, Y.; Guan, Z.; Li, H.; Ye, M.; Chen, X.; Shen, J.; Zhou, Y.; Shi, Z.L.; Zhou, P.; et al. SARS-CoV-2 triggers inflammatory responses and cell death through caspase-8 activation. Signal Transduct. Target. Ther. 2020, 5, 235. [Google Scholar] [CrossRef] [PubMed]
- Lee, W.; Ahn, J.H.; Park, H.H.; Kim, H.N.; Kim, H.; Yoo, Y.; Shin, H.; Hong, K.S.; Jang, J.G.; Park, C.G.; et al. COVID-19-activated SREBP2 disturbs cholesterol biosynthesis and leads to cytokine storm. Signal Transduct. Target. Ther. 2020, 5, 186. [Google Scholar] [CrossRef] [PubMed]
- Chen, H.; Kang, Y.; Duan, M.; Hou, T. Regulation Mechanism for the Binding between the SARS-CoV-2 Spike Protein and Host Angiotensin-Converting Enzyme II. J. Phys. Chem. Lett. 2021, 12, 6252–6261. [Google Scholar] [CrossRef] [PubMed]
- Menezes, M.C.S.; Pestana, D.V.S.; Gameiro, G.R.; da Silva, L.F.F.; Baron, E.; Rouby, J.J.; Auler, J.O.C., Jr. SARS-CoV-2 pneumonia-receptor binding and lung immunopathology: A narrative review. Crit. Care 2021, 25, 53. [Google Scholar] [CrossRef]
- Li, H.; Liu, L.; Zhang, D.; Xu, J.; Dai, H.; Tang, N.; Su, X.; Cao, B. SARS-CoV-2 and viral sepsis: Observations and hypotheses. Lancet 2020, 395, 1517–1520. [Google Scholar] [CrossRef]
- Patel, M.; Shahjin, F.; Cohen, J.D.; Hasan, M.; Machhi, J.; Chugh, H.; Singh, S.; Das, S.; Kulkarni, T.A.; Herskovitz, J.; et al. The immunopathobiology of SARS-CoV-2 infection. FEMS Microbiol. Rev. 2021, fuab035. [Google Scholar] [CrossRef]
- Azkur, A.K.; Akdis, M.; Azkur, D.; Sokolowska, M.; van de Veen, W.; Bruggen, M.C.; O’Mahony, L.; Gao, Y.; Nadeau, K.; Akdis, C.A. Immune response to SARS-CoV-2 and mechanisms of immunopathological changes in COVID-19. Allergy 2020, 75, 1564–1581. [Google Scholar] [CrossRef] [PubMed]
- Schijns, V.; Lavelle, E.C. Prevention and treatment of COVID-19 disease by controlled modulation of innate immunity. Eur. J. Immunol. 2020, 50, 932–938. [Google Scholar] [CrossRef]
- Chan, J.F.; To, K.K.; Tse, H.; Jin, D.Y.; Yuen, K.Y. Interspecies transmission and emergence of novel viruses: Lessons from bats and birds. Trends Microbiol. 2013, 21, 544–555. [Google Scholar] [CrossRef]
- Frieman, M.; Heise, M.; Baric, R. SARS coronavirus and innate immunity. Virus Res. 2008, 133, 101–112. [Google Scholar] [CrossRef]
- Jung, S.; Potapov, I.; Chillara, S.; Del Sol, A. Leveraging systems biology for predicting modulators of inflammation in patients with COVID-19. Sci. Adv. 2021, 7, eabe5735. [Google Scholar] [CrossRef] [PubMed]
- Di Gioacchino, A.; Sulc, P.; Komarova, A.V.; Greenbaum, B.D.; Monasson, R.; Cocco, S. The Heterogeneous Landscape and Early Evolution of Pathogen-Associated CpG Dinucleotides in SARS-CoV-2. Mol. Biol. Evol. 2021, 38, 2428–2445. [Google Scholar] [CrossRef]
- Choudhury, A.; Mukherjee, S. In silico studies on the comparative characterization of the interactions of SARS-CoV-2 spike glycoprotein with ACE-2 receptor homologs and human TLRs. J. Med. Virol. 2020, 92, 2105–2113. [Google Scholar] [CrossRef] [PubMed]
- Li, S.; Kuang, M.; Chen, L.; Li, Y.; Liu, S.; Du, H.; Cao, L.; You, F. The mitochondrial protein ERAL1 suppresses RNA virus infection by facilitating RIG-I-like receptor signaling. Cell Rep. 2021, 34, 108631. [Google Scholar] [CrossRef] [PubMed]
- Kienes, I.; Weidl, T.; Mirza, N.; Chamaillard, M.; Kufer, T.A. Role of NLRs in the Regulation of Type I Interferon Signaling, Host Defense and Tolerance to Inflammation. Int. J. Mol. Sci. 2021, 22, 1301. [Google Scholar] [CrossRef] [PubMed]
- Fitzgerald, K.A.; Kagan, J.C. Toll-like Receptors and the Control of Immunity. Cell 2020, 180, 1044–1066. [Google Scholar] [CrossRef] [PubMed]
- Zhao, Y.; Kuang, M.; Li, J.; Zhu, L.; Jia, Z.; Guo, X.; Hu, Y.; Kong, J.; Yin, H.; Wang, X.; et al. SARS-CoV-2 spike protein interacts with and activates TLR41. Cell Res. 2021, 31, 818–820. [Google Scholar] [CrossRef]
- Bhattacharya, M.; Sharma, A.R.; Mallick, B.; Sharma, G.; Lee, S.S.; Chakraborty, C. Immunoinformatics approach to understand molecular interaction between multi-epitopic regions of SARS-CoV-2 spike-protein with TLR4/MD-2 complex. Infect. Genet. Evol. 2020, 85, 104587. [Google Scholar] [CrossRef]
- Cantero-Navarro, E.; Fernandez-Fernandez, B.; Ramos, A.M.; Rayego-Mateos, S.; Rodrigues-Diez, R.R.; Sanchez-Nino, M.D.; Sanz, A.B.; Ruiz-Ortega, M.; Ortiz, A. Renin-angiotensin system and inflammation update. Mol. Cell Endocrinol. 2021, 529, 111254. [Google Scholar] [CrossRef]
- Zong, Z.; Zhang, Z.; Wu, L.; Zhang, L.; Zhou, F. The Functional Deubiquitinating Enzymes in Control of Innate Antiviral Immunity. Adv. Sci. 2021, 8, 2002484. [Google Scholar] [CrossRef]
- Li, L.; Acioglu, C.; Heary, R.F.; Elkabes, S. Role of astroglial toll-like receptors (TLRs) in central nervous system infections, injury and neurodegenerative diseases. Brain Behav. Immun. 2021, 91, 740–755. [Google Scholar] [CrossRef]
- Xia, S.; Zhong, Z.; Gao, B.; Vong, C.T.; Lin, X.; Cai, J.; Gao, H.; Chan, G.; Li, C. The important herbal pair for the treatment of COVID-19 and its possible mechanisms. Chin. Med. 2021, 16, 25. [Google Scholar] [CrossRef]
- Gianni, T.; Campadelli-Fiume, G. The epithelial alphavbeta3-integrin boosts the MYD88-dependent TLR2 signaling in response to viral and bacterial components. PLoS Pathog. 2014, 10, e1004477. [Google Scholar] [CrossRef] [Green Version]
- Qian, Y.; Lei, T.; Patel, P.; Lee, C.; Monaghan-Nichols, P.; Xin, H.B.; Qiu, J.; Fu, M. Direct activation of endothelial cells by SARS-CoV-2 nucleocapsid protein is blocked by Simvastatin. bioRxiv 2021. [Google Scholar] [CrossRef]
- Dosch, S.F.; Mahajan, S.D.; Collins, A.R. SARS coronavirus spike protein-induced innate immune response occurs via activation of the NF-kappaB pathway in human monocyte macrophages in vitro. Virus Res. 2009, 142, 19–27. [Google Scholar] [CrossRef] [PubMed]
- Imai, Y.; Kuba, K.; Neely, G.G.; Yaghubian-Malhami, R.; Perkmann, T.; van Loo, G.; Ermolaeva, M.; Veldhuizen, R.; Leung, Y.H.; Wang, H.; et al. Identification of oxidative stress and Toll-like receptor 4 signaling as a key pathway of acute lung injury. Cell 2008, 133, 235–249. [Google Scholar] [CrossRef]
- Mahla, R.S.; Reddy, M.C.; Prasad, D.V.; Kumar, H. Sweeten PAMPs: Role of Sugar Complexed PAMPs in Innate Immunity and Vaccine Biology. Front. Immunol. 2013, 4, 248. [Google Scholar] [CrossRef] [Green Version]
- Sallenave, J.M.; Guillot, L. Innate Immune Signaling and Proteolytic Pathways in the Resolution or Exacerbation of SARS-CoV-2 in COVID-19: Key Therapeutic Targets? Front. Immunol. 2020, 11, 1229. [Google Scholar] [CrossRef]
- Zhao, J.; Zhao, J.; Van Rooijen, N.; Perlman, S. Evasion by stealth: Inefficient immune activation underlies poor T cell response and severe disease in SARS-CoV-infected mice. PLoS Pathog. 2009, 5, e1000636. [Google Scholar] [CrossRef] [PubMed]
- Nakazono, A.; Nakamaru, Y.; Ramezanpour, M.; Kondo, T.; Watanabe, M.; Hatakeyama, S.; Kimura, S.; Honma, A.; Wormald, P.J.; Vreugde, S.; et al. Fluticasone Propionate Suppresses Poly(I:C)-Induced ACE2 in Primary Human Nasal Epithelial Cells. Front. Cell Infect. Microbiol. 2021, 11, 655666. [Google Scholar] [CrossRef]
- Meas, H.Z.; Haug, M.; Beckwith, M.S.; Louet, C.; Ryan, L.; Hu, Z.; Landskron, J.; Nordbo, S.A.; Tasken, K.; Yin, H.; et al. Sensing of HIV-1 by TLR8 activates human T cells and reverses latency. Nat. Commun. 2020, 11, 147. [Google Scholar] [CrossRef]
- Barrat, F.J.; Su, L. A pathogenic role of plasmacytoid dendritic cells in autoimmunity and chronic viral infection. J. Exp. Med. 2019, 216, 1974–1985. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Li, Y.; Chen, M.; Cao, H.; Zhu, Y.; Zheng, J.; Zhou, H. Extraordinary GU-rich single-strand RNA identified from SARS coronavirus contributes an excessive innate immune response. Microbes Infect. 2013, 15, 88–95. [Google Scholar] [CrossRef] [PubMed]
- Lee, I.H.; Lee, J.W.; Kong, S.W. A survey of genetic variants in SARS-CoV-2 interacting domains of ACE2, TMPRSS2 and TLR3/7/8 across populations. Infect. Genet. Evol. 2020, 85, 104507. [Google Scholar] [CrossRef]
- Angelopoulou, A.; Alexandris, N.; Konstantinou, E.; Mesiakaris, K.; Zanidis, C.; Farsalinos, K.; Poulas, K. Imiquimod—A toll like receptor 7 agonist—Is an ideal option for management of COVID 19. Environ. Res. 2020, 188, 109858. [Google Scholar] [CrossRef] [PubMed]
- Moreno-Eutimio, M.A.; Lopez-Macias, C.; Pastelin-Palacios, R. Bioinformatic analysis and identification of single-stranded RNA sequences recognized by TLR7/8 in the SARS-CoV-2, SARS-CoV, and MERS-CoV genomes. Microbes Infect. 2020, 22, 226–229. [Google Scholar] [CrossRef]
- Sharma, J.; Parsai, K.; Raghuwanshi, P.; Ali, S.A.; Tiwari, V.; Bhargava, A.; Mishra, P.K. Emerging role of mitochondria in airborne particulate matter-induced immunotoxicity. Environ. Pollut. 2021, 270, 116242. [Google Scholar] [CrossRef] [PubMed]
- Lai, C.Y.; Su, Y.W.; Lin, K.I.; Hsu, L.C.; Chuang, T.H. Natural Modulators of Endosomal Toll-Like Receptor-Mediated Psoriatic Skin Inflammation. J. Immunol. Res. 2017, 2017, 7807313. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Myong, S.; Cui, S.; Cornish, P.V.; Kirchhofer, A.; Gack, M.U.; Jung, J.U.; Hopfner, K.P.; Ha, T. Cytosolic viral sensor RIG-I is a 5′-triphosphate-dependent translocase on double-stranded RNA. Science 2009, 323, 1070–1074. [Google Scholar] [CrossRef] [Green Version]
- Chiang, C.; Liu, G.; Gack, M.U. Viral Evasion of RIG-I-Like Receptor-Mediated Immunity through Dysregulation of Ubiquitination and ISGylation. Viruses 2021, 13, 182. [Google Scholar] [CrossRef]
- Errett, J.S.; Gale, M. Emerging complexity and new roles for the RIG-I-like receptors in innate antiviral immunity. Virol. Sin. 2015, 30, 163–173. [Google Scholar] [CrossRef] [PubMed]
- Loo, Y.M.; Gale, M., Jr. Immune signaling by RIG-I-like receptors. Immunity 2011, 34, 680–692. [Google Scholar] [CrossRef] [Green Version]
- Esser-Nobis, K.; Hatfield, L.D.; Gale, M., Jr. Spatiotemporal dynamics of innate immune signaling via RIG-I-like receptors. Proc. Natl. Acad. Sci. USA 2020, 117, 15778–15788. [Google Scholar] [CrossRef] [PubMed]
- Wu, J.; Shi, Y.; Pan, X.; Wu, S.; Hou, R.; Zhang, Y.; Zhong, T.; Tang, H.; Du, W.; Wang, L.; et al. SARS-CoV-2 ORF9b inhibits RIG-I-MAVS antiviral signaling by interrupting K63-linked ubiquitination of NEMO. Cell Rep. 2021, 34, 108761. [Google Scholar] [CrossRef] [PubMed]
- Yang, D.; Geng, T.; Harrison, A.G.; Wang, P. Differential roles of RIG-I-like receptors in SARS-CoV-2 infection. bioRxiv 2021. [Google Scholar] [CrossRef]
- Onomoto, K.; Onoguchi, K.; Yoneyama, M. Regulation of RIG-I-like receptor-mediated signaling: Interaction between host and viral factors. Cell Mol. Immunol. 2021, 18, 539–555. [Google Scholar] [CrossRef] [PubMed]
- Stuart, J.D.; Holm, G.H.; Boehme, K.W. Differential Delivery of Genomic Double-Stranded RNA Causes Reovirus Strain-Specific Differences in Interferon Regulatory Factor 3 Activation. J. Virol. 2018, 92, e01947-17. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lei, Y.; Moore, C.B.; Liesman, R.M.; O’Connor, B.P.; Bergstralh, D.T.; Chen, Z.J.; Pickles, R.J.; Ting, J.P. MAVS-mediated apoptosis and its inhibition by viral proteins. PLoS ONE 2009, 4, e5466. [Google Scholar] [CrossRef] [PubMed]
- Kash, J.C.; Muhlberger, E.; Carter, V.; Grosch, M.; Perwitasari, O.; Proll, S.C.; Thomas, M.J.; Weber, F.; Klenk, H.D.; Katze, M.G. Global suppression of the host antiviral response by Ebola- and Marburgviruses: Increased antagonism of the type I interferon response is associated with enhanced virulence. J. Virol. 2006, 80, 3009–3020. [Google Scholar] [CrossRef] [Green Version]
- Zheng, Y.; Zhuang, M.W.; Han, L.; Zhang, J.; Nan, M.L.; Zhan, P.; Kang, D.; Liu, X.; Gao, C.; Wang, P.H. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) membrane (M) protein inhibits type I and III interferon production by targeting RIG-I/MDA-5 signaling. Signal Transduct. Target. Ther. 2020, 5, 299. [Google Scholar] [CrossRef] [PubMed]
- Abe, T.; Marutani, Y.; Shoji, I. Cytosolic DNA-sensing immune response and viral infection. Microbiol. Immunol. 2019, 63, 51–64. [Google Scholar] [CrossRef] [Green Version]
- Maringer, K.; Fernandez-Sesma, A. Message in a bottle: Lessons learned from antagonism of STING signalling during RNA virus infection. Cytokine Growth Factor Rev. 2014, 25, 669–679. [Google Scholar] [CrossRef] [Green Version]
- Ma, Z.; Damania, B. The cGAS-STING Defense Pathway and Its Counteraction by Viruses. Cell Host Microbe 2016, 19, 150–158. [Google Scholar] [CrossRef] [PubMed]
- Berthelot, J.M.; Liote, F.; Maugars, Y.; Sibilia, J. Lymphocyte Changes in Severe COVID-19: Delayed Over-Activation of STING? Front. Immunol. 2020, 11, 607069. [Google Scholar] [CrossRef]
- Barber, G.N. STING: Infection, inflammation and cancer. Nat. Rev. Immunol. 2015, 15, 760–770. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Li, T.; Chen, Z.J. The cGAS-cGAMP-STING pathway connects DNA damage to inflammation, senescence, and cancer. J. Exp. Med. 2018, 215, 1287–1299. [Google Scholar] [CrossRef] [PubMed]
- Hoong, B.Y.D.; Gan, Y.H.; Liu, H.; Chen, E.S. cGAS-STING pathway in oncogenesis and cancer therapeutics. Oncotarget 2020, 11, 2930–2955. [Google Scholar] [CrossRef] [PubMed]
- Humphries, F.; Shmuel-Galia, L.; Jiang, Z.; Wilson, R.; Landis, P.; Ng, S.L.; Fitzgerald, K.A. A diamidobenzimidazole STING agonist protects against SARS-CoV-2 infection. Sci. Immunol. 2021, 6, eabi9002. [Google Scholar] [CrossRef] [PubMed]
- Aguirre, S.; Luthra, P.; Sanchez-Aparicio, M.T.; Maestre, A.M.; Patel, J.; Lamothe, F.; Fredericks, A.C.; Tripathi, S.; Zhu, T.; Pintado-Silva, J.; et al. Dengue virus NS2B protein targets cGAS for degradation and prevents mitochondrial DNA sensing during infection. Nat. Microbiol. 2017, 2, 17037. [Google Scholar] [CrossRef] [PubMed]
- Schoggins, J.W.; MacDuff, D.A.; Imanaka, N.; Gainey, M.D.; Shrestha, B.; Eitson, J.L.; Mar, K.B.; Richardson, R.B.; Ratushny, A.V.; Litvak, V.; et al. Pan-viral specificity of IFN-induced genes reveals new roles for cGAS in innate immunity. Nature 2014, 505, 691–695. [Google Scholar] [CrossRef]
- Wang, J.; Li, P.; Yu, Y.; Fu, Y.; Jiang, H.; Lu, M.; Sun, Z.; Jiang, S.; Lu, L.; Wu, M.X. Pulmonary surfactant-biomimetic nanoparticles potentiate heterosubtypic influenza immunity. Science 2020, 367, eaau0810. [Google Scholar] [CrossRef]
- Rui, Y.; Su, J.; Shen, S.; Hu, Y.; Huang, D.; Zheng, W.; Lou, M.; Shi, Y.; Wang, M.; Chen, S.; et al. Unique and complementary suppression of cGAS-STING and RNA sensing- triggered innate immune responses by SARS-CoV-2 proteins. Signal Transduct. Target. Ther. 2021, 6, 123. [Google Scholar] [CrossRef] [PubMed]
- Sun, L.; Xing, Y.; Chen, X.; Zheng, Y.; Yang, Y.; Nichols, D.B.; Clementz, M.A.; Banach, B.S.; Li, K.; Baker, S.C.; et al. Coronavirus papain-like proteases negatively regulate antiviral innate immune response through disruption of STING-mediated signaling. PLoS ONE 2012, 7, e30802. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Clementz, M.A.; Chen, Z.; Banach, B.S.; Wang, Y.; Sun, L.; Ratia, K.; Baez-Santos, Y.M.; Wang, J.; Takayama, J.; Ghosh, A.K.; et al. Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases. J. Virol. 2010, 84, 4619–4629. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ni, G.; Ma, Z.; Damania, B. cGAS and STING: At the intersection of DNA and RNA virus-sensing networks. PLoS Pathog. 2018, 14, e1007148. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Berthelot, J.M.; Drouet, L.; Liote, F. Kawasaki-like diseases and thrombotic coagulopathy in COVID-19: Delayed over-activation of the STING pathway? Emerg. Microbes Infect. 2020, 9, 1514–1522. [Google Scholar] [CrossRef] [PubMed]
- Qiao, Y.; Zhu, S.; Deng, S.; Zou, S.S.; Gao, B.; Zang, G.; Wu, J.; Jiang, Y.; Liu, Y.J.; Chen, J. Human Cancer Cells Sense Cytosolic Nucleic Acids Through the RIG-I-MAVS Pathway and cGAS-STING Pathway. Front. Cell Dev. Biol. 2020, 8, 606001. [Google Scholar] [CrossRef]
- Mdkhana, B.; Saheb Sharif-Askari, N.; Ramakrishnan, R.K.; Goel, S.; Hamid, Q.; Halwani, R. Nucleic Acid-Sensing Pathways During SARS-CoV-2 Infection: Expectations versus Reality. J. Inflamm. Res. 2021, 14, 199–216. [Google Scholar] [CrossRef]
- Levy, R.; Bastard, P.; Lanternier, F.; Lecuit, M.; Zhang, S.Y.; Casanova, J.L. Correction to: IFN-alpha2a Therapy in Two Patients with Inborn Errors of TLR3 and IRF3 Infected with SARS-CoV-2. J. Clin. Immunol. 2021, 41, 28. [Google Scholar] [CrossRef] [PubMed]
- Spel, L.; Martinon, F. Detection of viruses by inflammasomes. Curr. Opin. Virol. 2021, 46, 59–64. [Google Scholar] [CrossRef] [PubMed]
- Huang, H.; Wang, J.; Liu, Z.; Gao, F. The angiotensin-converting enzyme 2/angiotensin (1-7)/mas axis protects against pyroptosis in LPS-induced lung injury by inhibiting NLRP3 activation. Arch. Biochem. Biophys. 2020, 693, 108562. [Google Scholar] [CrossRef] [PubMed]
- Ratajczak, M.Z.; Bujko, K.; Ciechanowicz, A.; Sielatycka, K.; Cymer, M.; Marlicz, W.; Kucia, M. SARS-CoV-2 Entry Receptor ACE2 Is Expressed on Very Small CD45(-) Precursors of Hematopoietic and Endothelial Cells and in Response to Virus Spike Protein Activates the Nlrp3 Inflammasome. Stem Cell Rev. Rep. 2021, 17, 266–277. [Google Scholar] [CrossRef]
- You, Y.; Huang, Y.; Wang, D.; Li, Y.; Wang, G.; Jin, S.; Zhu, X.; Wu, B.; Du, X.; Li, X. Angiotensin (1–7) inhibits arecoline-induced migration and collagen synthesis in human oral myofibroblasts via inhibiting NLRP3 inflammasome activation. J. Cell Physiol. 2019, 234, 4668–4680. [Google Scholar] [CrossRef] [PubMed]
- Ratajczak, M.Z.; Kucia, M. SARS-CoV-2 infection and overactivation of Nlrp3 inflammasome as a trigger of cytokine “storm” and risk factor for damage of hematopoietic stem cells. Leukemia 2020, 34, 1726–1729. [Google Scholar] [CrossRef]
- Zhao, C.; Zhao, W. NLRP3 Inflammasome-A Key Player in Antiviral Responses. Front. Immunol. 2020, 11, 211. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Van Den Eeckhout, B.; Van Hoecke, L.; Burg, E.; Van Lint, S.; Peelman, F.; Kley, N.; Uze, G.; Saelens, X.; Tavernier, J.; Gerlo, S. Specific targeting of IL-1beta activity to CD8(+) T cells allows for safe use as a vaccine adjuvant. NPJ Vaccines 2020, 5, 64. [Google Scholar] [CrossRef]
- Ichinohe, T.; Pang, I.K.; Iwasaki, A. Influenza virus activates inflammasomes via its intracellular M2 ion channel. Nat. Immunol. 2010, 11, 404–410. [Google Scholar] [CrossRef]
- Thomas, P.G.; Dash, P.; Aldridge, J.R., Jr.; Ellebedy, A.H.; Reynolds, C.; Funk, A.J.; Martin, W.J.; Lamkanfi, M.; Webby, R.J.; Boyd, K.L.; et al. The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1. Immunity 2009, 30, 566–575. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Chen, I.Y.; Moriyama, M.; Chang, M.F.; Ichinohe, T. Severe Acute Respiratory Syndrome Coronavirus Viroporin 3a Activates the NLRP3 Inflammasome. Front. Microbiol. 2019, 10, 50. [Google Scholar] [CrossRef] [Green Version]
- Triantafilou, K.; Triantafilou, M. Ion flux in the lung: Virus-induced inflammasome activation. Trends Microbiol. 2014, 22, 580–588. [Google Scholar] [CrossRef] [PubMed]
- DeDiego, M.L.; Nieto-Torres, J.L.; Jimenez-Guardeno, J.M.; Regla-Nava, J.A.; Castano-Rodriguez, C.; Fernandez-Delgado, R.; Usera, F.; Enjuanes, L. Coronavirus virulence genes with main focus on SARS-CoV envelope gene. Virus Res. 2014, 194, 124–137. [Google Scholar] [CrossRef]
- Mesotten, D.; Meijs, D.A.M.; van Bussel, B.C.T.; Stessel, B.; Mehagnoul-Schipper, J.; Hana, A.; Scheeren, C.I.E.; Strauch, U.; van de Poll, M.C.G.; Ghossein-Doha, C.; et al. Differences and Similarities Among Coronavirus Disease 2019 Patients Treated in Seven ICUs in Three Countries Within One Region: An Observational Cohort Study. Crit. Care Med. 2021. [Google Scholar] [CrossRef] [PubMed]
- Asarnow, D.; Wang, B.; Lee, W.H.; Hu, Y.; Huang, C.W.; Faust, B.; Ng, P.M.L.; Ngoh, E.Z.X.; Bohn, M.; Bulkley, D.; et al. Structural insight into SARS-CoV-2 neutralizing antibodies and modulation of syncytia. Cell 2021, 184, 3192–3204.e3116. [Google Scholar] [CrossRef] [PubMed]
- Lu, Q.; Liu, J.; Zhao, S.; Gomez Castro, M.F.; Laurent-Rolle, M.; Dong, J.; Ran, X.; Damani-Yokota, P.; Tang, H.; Karakousi, T.; et al. SARS-CoV-2 exacerbates proinflammatory responses in myeloid cells through C-type lectin receptors and Tweety family member 2. Immunity 2021, 54, 1304–1319.e1309. [Google Scholar] [CrossRef] [PubMed]
- Savarino, A.; Boelaert, J.R.; Cassone, A.; Majori, G.; Cauda, R. Effects of chloroquine on viral infections: An old drug against today’s diseases? Lancet Infect. Dis. 2003, 3, 722–727. [Google Scholar] [CrossRef]
- Ma, L.L.; Liu, H.M.; Liu, X.M.; Yuan, X.Y.; Xu, C.; Wang, F.; Lin, J.Z.; Xu, R.C.; Zhang, D.K. Screening S protein—ACE2 blockers from natural products: Strategies and advances in the discovery of potential inhibitors of COVID-19. Eur. J. Med. Chem. 2021, 226, 113857. [Google Scholar] [CrossRef]
- Gies, V.; Bekaddour, N.; Dieudonne, Y.; Guffroy, A.; Frenger, Q.; Gros, F.; Rodero, M.P.; Herbeuval, J.P.; Korganow, A.S. Beyond Anti-viral Effects of Chloroquine/Hydroxychloroquine. Front. Immunol. 2020, 11, 1409. [Google Scholar] [CrossRef] [PubMed]
- Ortiz, M.E.; Thurman, A.; Pezzulo, A.A.; Leidinger, M.R.; Klesney-Tait, J.A.; Karp, P.H.; Tan, P.; Wohlford-Lenane, C.; McCray, P.B., Jr.; Meyerholz, D.K. Heterogeneous expression of the SARS-Coronavirus-2 receptor ACE2 in the human respiratory tract. EBioMedicine 2020, 60, 102976. [Google Scholar] [CrossRef]
- Devaux, C.A.; Rolain, J.M.; Colson, P.; Raoult, D. New insights on the antiviral effects of chloroquine against coronavirus: What to expect for COVID-19? Int. J. Antimicrob. Agents 2020, 55, 105938. [Google Scholar] [CrossRef]
- Wang, N.; Han, S.; Liu, R.; Meng, L.; He, H.; Zhang, Y.; Wang, C.; Lv, Y.; Wang, J.; Li, X.; et al. Chloroquine and hydroxychloroquine as ACE2 blockers to inhibit viropexis of 2019-nCoV Spike pseudotyped virus. Phytomedicine 2020, 79, 153333. [Google Scholar] [CrossRef] [PubMed]
- Yan, Y.; Zou, Z.; Sun, Y.; Li, X.; Xu, K.F.; Wei, Y.; Jin, N.; Jiang, C. Anti-malaria drug chloroquine is highly effective in treating avian influenza A H5N1 virus infection in an animal model. Cell Res. 2013, 23, 300–302. [Google Scholar] [CrossRef] [Green Version]
- Mitja, O.; Corbacho-Monne, M.; Ubals, M.; Alemany, A.; Suner, C.; Tebe, C.; Tobias, A.; Penafiel, J.; Ballana, E.; Perez, C.A.; et al. A Cluster-Randomized Trial of Hydroxychloroquine for Prevention of COVID-19. N. Engl. J. Med. 2021, 384, 417–427. [Google Scholar] [CrossRef]
- Fried, M.W.; Crawford, J.M.; Mospan, A.R.; Watkins, S.E.; Munoz, B.; Zink, R.C.; Elliott, S.; Burleson, K.; Landis, C.; Reddy, K.R.; et al. Patient Characteristics and Outcomes of 11 721 Patients with Coronavirus Disease 2019 (COVID-19) Hospitalized Across the United States. Clin. Infect. Dis. 2021, 72, e558–e565. [Google Scholar] [CrossRef]
- Abella, B.S.; Jolkovsky, E.L.; Biney, B.T.; Uspal, J.E.; Hyman, M.C.; Frank, I.; Hensley, S.E.; Gill, S.; Vogl, D.T.; Maillard, I.; et al. Efficacy and Safety of Hydroxychloroquine vs Placebo for Pre-exposure SARS-CoV-2 Prophylaxis Among Health Care Workers: A Randomized Clinical Trial. JAMA Intern. Med. 2021, 181, 195–202. [Google Scholar] [CrossRef]
- Barnabas, R.V.; Brown, E.R.; Bershteyn, A.; Stankiewicz Karita, H.C.; Johnston, C.; Thorpe, L.E.; Kottkamp, A.; Neuzil, K.M.; Laufer, M.K.; Deming, M.; et al. Hydroxychloroquine as Postexposure Prophylaxis to Prevent Severe Acute Respiratory Syndrome Coronavirus 2 Infection: A Randomized Trial. Ann. Intern. Med. 2021, 174, 344–352. [Google Scholar] [CrossRef] [PubMed]
- Arabi, Y.M.; Gordon, A.C.; Derde, L.P.G.; Nichol, A.D.; Murthy, S.; Beidh, F.A.; Annane, D.; Swaidan, L.A.; Beane, A.; Beasley, R.; et al. Lopinavir-ritonavir and hydroxychloroquine for critically ill patients with COVID-19: REMAP-CAP randomized controlled trial. Intensive Care Med. 2021, 47, 867–886. [Google Scholar] [CrossRef]
- Magagnoli, J.; Narendran, S.; Pereira, F.; Cummings, T.; Hardin, J.W.; Sutton, S.S.; Ambati, J. Outcomes of hydroxychloroquine usage in United States veterans hospitalized with COVID-19. medRxiv 2020, 1, 114–127.e3. [Google Scholar] [CrossRef] [PubMed]
- Lebek, S.; Tafelmeier, M.; Messmann, R.; Provaznik, Z.; Schmid, C.; Maier, L.S.; Birner, C.; Arzt, M.; Wagner, S. Angiotensin-converting enzyme inhibitor/angiotensin II receptor blocker treatment and haemodynamic factors are associated with increased cardiac mRNA expression of angiotensin-converting enzyme 2 in patients with cardiovascular disease. Eur. J. Heart Fail. 2020, 22, 2248–2257. [Google Scholar] [CrossRef] [PubMed]
- Neyrinck, A.P.; Matthay, M.A. The role of angiotensin-converting enzyme inhibition in endotoxin-induced lung injury in rats. Crit. Care Med. 2009, 37, 776–777. [Google Scholar] [CrossRef] [PubMed]
- Melissa Hallow, K.; Dave, I. RAAS Blockade and COVID-19: Mechanistic Modeling of Mas and AT1 Receptor Occupancy as Indicators of Pro-Inflammatory and Anti-Inflammatory Balance. Clin. Pharmacol. Ther. 2021, 109, 1092–1103. [Google Scholar] [CrossRef] [PubMed]
- Yisireyili, M.; Uchida, Y.; Yamamoto, K.; Nakayama, T.; Cheng, X.W.; Matsushita, T.; Nakamura, S.; Murohara, T.; Takeshita, K. Angiotensin receptor blocker irbesartan reduces stress-induced intestinal inflammation via AT1a signaling and ACE2-dependent mechanism in mice. Brain Behav. Immun. 2018, 69, 167–179. [Google Scholar] [CrossRef]
- Hallaj, S.; Ghorbani, A.; Mousavi-Aghdas, S.A.; Mirza-Aghazadeh-Attari, M.; Sevbitov, A.; Hashemi, V.; Hallaj, T.; Jadidi-Niaragh, F. Angiotensin-converting enzyme as a new immunologic target for the new SARS-CoV-2. Immunol. Cell Biol. 2021, 99, 192–205. [Google Scholar] [CrossRef]
- Kriszta, G.; Kriszta, Z.; Vancsa, S.; Hegyi, P.J.; Frim, L.; Eross, B.; Hegyi, P.; Petho, G.; Pinter, E. Effects of Angiotensin-Converting Enzyme Inhibitors and Angiotensin Receptor Blockers on Angiotensin-Converting Enzyme 2 Levels: A Comprehensive Analysis Based on Animal Studies. Front. Pharmacol. 2021, 12, 619524. [Google Scholar] [CrossRef]
- Zhang, P.; Zhu, L.; Cai, J.; Lei, F.; Qin, J.J.; Xie, J.; Liu, Y.M.; Zhao, Y.C.; Huang, X.; Lin, L.; et al. Association of Inpatient Use of Angiotensin-Converting Enzyme Inhibitors and Angiotensin II Receptor Blockers with Mortality Among Patients with Hypertension Hospitalized with COVID-19. Circ. Res. 2020, 126, 1671–1681. [Google Scholar] [CrossRef]
- Zhuang, M.W.; Cheng, Y.; Zhang, J.; Jiang, X.M.; Wang, L.; Deng, J.; Wang, P.H. Increasing host cellular receptor-angiotensin-converting enzyme 2 expression by coronavirus may facilitate 2019-nCoV (or SARS-CoV-2) infection. J. Med. Virol. 2020, 92, 2693–2701. [Google Scholar] [CrossRef]
- Mehta, N.; Kalra, A.; Nowacki, A.S.; Anjewierden, S.; Han, Z.; Bhat, P.; Carmona-Rubio, A.E.; Jacob, M.; Procop, G.W.; Harrington, S.; et al. Association of Use of Angiotensin-Converting Enzyme Inhibitors and Angiotensin II Receptor Blockers with Testing Positive for Coronavirus Disease 2019 (COVID-19). JAMA Cardiol. 2020, 5, 1020–1026. [Google Scholar] [CrossRef] [PubMed]
- Guzik, T.J.; Mohiddin, S.A.; Dimarco, A.; Patel, V.; Savvatis, K.; Marelli-Berg, F.M.; Madhur, M.S.; Tomaszewski, M.; Maffia, P.; D’Acquisto, F.; et al. COVID-19 and the cardiovascular system: Implications for risk assessment, diagnosis, and treatment options. Cardiovasc. Res. 2020, 116, 1666–1687. [Google Scholar] [CrossRef] [PubMed]
- Gross, S.; Jahn, C.; Cushman, S.; Bar, C.; Thum, T. SARS-CoV-2 receptor ACE2-dependent implications on the cardiovascular system: From basic science to clinical implications. J. Mol. Cell Cardiol. 2020, 144, 47–53. [Google Scholar] [CrossRef]
- Hemnes, A.R.; Rathinasabapathy, A.; Austin, E.A.; Brittain, E.L.; Carrier, E.J.; Chen, X.; Fessel, J.P.; Fike, C.D.; Fong, P.; Fortune, N.; et al. A potential therapeutic role for angiotensin-converting enzyme 2 in human pulmonary arterial hypertension. Eur. Respir. J. 2018, 51, 1702638. [Google Scholar] [CrossRef]
- Rey-Parra, G.J.; Vadivel, A.; Coltan, L.; Hall, A.; Eaton, F.; Schuster, M.; Loibner, H.; Penninger, J.M.; Kassiri, Z.; Oudit, G.Y.; et al. Angiotensin converting enzyme 2 abrogates bleomycin-induced lung injury. J. Mol. Med. 2012, 90, 637–647. [Google Scholar] [CrossRef] [PubMed]
- Hoepel, W.; Chen, H.J.; Geyer, C.E.; Allahverdiyeva, S.; Manz, X.D.; de Taeye, S.W.; Aman, J.; Mes, L.; Steenhuis, M.; Griffith, G.R.; et al. High titers and low fucosylation of early human anti-SARS-CoV-2 IgG promote inflammation by alveolar macrophages. Sci. Transl. Med. 2021, 13, eabf8654. [Google Scholar] [CrossRef]
- Monteil, V.; Kwon, H.; Prado, P.; Hagelkruys, A.; Wimmer, R.A.; Stahl, M.; Leopoldi, A.; Garreta, E.; Hurtado Del Pozo, C.; Prosper, F.; et al. Inhibition of SARS-CoV-2 Infections in Engineered Human Tissues Using Clinical-Grade Soluble Human ACE2. Cell 2020, 181, 905–913.e907. [Google Scholar] [CrossRef]
- Huang, K.Y.; Lin, M.S.; Kuo, T.C.; Chen, C.L.; Lin, C.C.; Chou, Y.C.; Chao, T.L.; Pang, Y.H.; Kao, H.C.; Huang, R.S.; et al. Humanized COVID-19 decoy antibody effectively blocks viral entry and prevents SARS-CoV-2 infection. EMBO Mol. Med. 2021, 13, e12828. [Google Scholar] [CrossRef]
- Zhang, Y.; Leung, D.Y.; Goleva, E. Anti-inflammatory and corticosteroid-enhancing actions of vitamin D in monocytes of patients with steroid-resistant and those with steroid-sensitive asthma. J. Allergy Clin. Immunol. 2014, 133, 1744–1752.e1741. [Google Scholar] [CrossRef] [Green Version]
- Bassatne, A.; Basbous, M.; Chakhtoura, M.; El Zein, O.; Rahme, M.; El-Hajj Fuleihan, G. The link between COVID-19 and VItamin D (VIVID): A systematic review and meta-analysis. Metabolism 2021, 119, 154753. [Google Scholar] [CrossRef]
- Peng, M.Y.; Liu, W.C.; Zheng, J.Q.; Lu, C.L.; Hou, Y.C.; Zheng, C.M.; Song, J.Y.; Lu, K.C.; Chao, Y.C. Immunological Aspects of SARS-CoV-2 Infection and the Putative Beneficial Role of Vitamin-D. Int. J. Mol. Sci. 2021, 22, 5251. [Google Scholar] [CrossRef] [PubMed]
- Li, Y.C.; Qiao, G.; Uskokovic, M.; Xiang, W.; Zheng, W.; Kong, J. Vitamin D: A negative endocrine regulator of the renin-angiotensin system and blood pressure. J. Steroid Biochem. Mol. Biol. 2004, 89–90, 387–392. [Google Scholar] [CrossRef] [PubMed]
- Li, Y.C.; Kong, J.; Wei, M.; Chen, Z.F.; Liu, S.Q.; Cao, L.P. 1,25-Dihydroxyvitamin D(3) is a negative endocrine regulator of the renin-angiotensin system. J. Clin. Investig. 2002, 110, 229–238. [Google Scholar] [CrossRef] [PubMed]
- Xu, S.; Chen, Y.H.; Tan, Z.X.; Xie, D.D.; Zhang, C.; Xia, M.Z.; Wang, H.; Zhao, H.; Xu, D.X.; Yu, D.X. Vitamin D3 pretreatment alleviates renal oxidative stress in lipopolysaccharide-induced acute kidney injury. J. Steroid Biochem. Mol. Biol. 2015, 152, 133–141. [Google Scholar] [CrossRef] [PubMed]
- Mendonca, P.; Soliman, K.F.A. Flavonoids Activation of the Transcription Factor Nrf2 as a Hypothesis Approach for the Prevention and Modulation of SARS-CoV-2 Infection Severity. Antioxidants 2020, 9, 659. [Google Scholar] [CrossRef] [PubMed]
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Qu, L.; Chen, C.; Yin, T.; Fang, Q.; Hong, Z.; Zhou, R.; Tang, H.; Dong, H. ACE2 and Innate Immunity in the Regulation of SARS-CoV-2-Induced Acute Lung Injury: A Review. Int. J. Mol. Sci. 2021, 22, 11483. https://doi.org/10.3390/ijms222111483
Qu L, Chen C, Yin T, Fang Q, Hong Z, Zhou R, Tang H, Dong H. ACE2 and Innate Immunity in the Regulation of SARS-CoV-2-Induced Acute Lung Injury: A Review. International Journal of Molecular Sciences. 2021; 22(21):11483. https://doi.org/10.3390/ijms222111483
Chicago/Turabian StyleQu, Lihua, Chao Chen, Tong Yin, Qian Fang, Zizhan Hong, Rui Zhou, Hongbin Tang, and Huifen Dong. 2021. "ACE2 and Innate Immunity in the Regulation of SARS-CoV-2-Induced Acute Lung Injury: A Review" International Journal of Molecular Sciences 22, no. 21: 11483. https://doi.org/10.3390/ijms222111483