Molecular recognition in the infection, replication, and transmission of COVID-19-causing SARS-CoV-2: an emerging interface of infectious disease, biological chemistry, and nanoscience
Source abstract
Abstract
Abstract A coronavirus (CoV) commonly known as SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) and causing COVID-19 (coronavirus disease of 2019) has become a pandemic following an outbreak in Wuhan. Although mutations in the SARS-CoV-2 spike glycoprotein (SGP) are obvious from comparative genome studies, the novel infectious nature of the virus, its new varients detected in the UK, and outside and recovery–death ratios of COVID-19 inspired us to review the mechanisms of the infection, replication, release, and transmission of progeny virions and the immune response in the host cell. In addition to the specificity of SARS-CoV-2 binding to angiotensin-converting enzyme 2 receptor and transmembrane protease serine 2, the varied symptoms and severity of the infection by the original and mutated forms of the virus suggest the significance of correlating the host innate and adaptive immunity with the binding of the virus to the mannose receptor via lipopolysaccharides (LPSs), toll-like receptors via LPS/proteins/RNA, and sialic acid (Sia) via hemagglutinin, or sugar-acid segments of glycans. HA-to-Sia binding is considered based on the innate Sia N-acetylneuraminic acid and the acquired Sia N-glycolylneuraminic acid in the epithelial cells and the sialidase/neuraminidase- or esterase-hydrolyzed release and transmission of CoVs. Furthermore, the cytokine storms common to aged humans infected with SARS-CoV-2 and aged macaques infected with SARS-CoV encourage us to articulate the mechanism by which the nuclear capsid protein and RNAs bypass the pattern recognition-induced secretion of interferons (IFNs), which stimulate IFN genes through the Janus-activated kinase-signal transducer and activator of a transcription pathway, leading to the secretion of antiviral proteins such as myxovirus resistance protein A/B. By considering the complexities of the structure, and the infectious nature of the virus and the structures and functions of the molecules involved in CoV infection, replication, and immune response, a new interface among virology, immunology, chemistry, imaging technology, drug delivery, and nanoscience is proposed and will be developed. This interface can be an essential platform for researchers, technologists, and physicians to collaborate and develop vaccines and medicines against COVID-19 and other pandemics in the future.
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Research context
OpenAlex topics: SARS-CoV-2 and COVID-19 Research · Viral Infections and Outbreaks Research · interferon and immune responses
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References (100+)
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1. Wrapp, D. et al. Cryo-EM structure of the 2019-NCoV spike in the prefusion conformation. Science 367, 1260–1263 (2020).10.1126/science.abb2507 ↗
2. Goldsmith, C. S., Miller, S. E., Martines, R. B., Bullock, H. A. & Zaki, S. R. Electron microscopy of SARS-CoV-2: a challenging task. Lancet 395, e99 (2020).10.1016/S0140-6736(20)31188-0 ↗
3. To, K. K. W. et al. Temporal profiles of viral load in posterior oropharyngeal saliva samples and serum antibody responses during infection by SARS-CoV-2: an observational cohort study. Lancet Infect. Dis. 20, 565–574 (2020).10.1016/S1473-3099(20)30196-1 ↗
4. Lu, R. et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet 395, 565–574 (2020).10.1016/S0140-6736(20)30251-8 ↗
5. Jeffers, S. A. et al. CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus. Proc. Natl Acad. Sci. USA 101, 15748–15753 (2004).10.1073/pnas.0403812101 ↗
6. Agostini, M. L. et al. Coronavirus susceptibility to the antiviral remdesivir (GS-5734) is mediated by the viral polymerase and the proofreading exoribonuclease. MBio 9, 1–15 (2018).10.1128/mBio.00221-18 ↗
7. Zhang, T., Wu, Q. & Zhang, Z. Probable Pangolin origin of SARS-CoV-2 associated with the COVID-19 outbreak. Curr. Biol. 30, 1346–1351 (2020).10.1016/j.cub.2020.03.022 ↗
8. Andersen, K. G., Rambaut, A., Lipkin, W. I., Holmes, E. C. & Garry, R. F. The proximal origin of SARS-CoV-2. Nat. Med. 26, 450–452 (2020).10.1038/s41591-020-0820-9 ↗
9. Angeletti, S. et al. COVID-2019: the role of the Nsp2 and Nsp3 in its pathogenesis. J. Med. Virol. 92, 584–588 (2020).10.1002/jmv.25719 ↗
10. Liu, Z. et al. Composition and divergence of coronavirus spike proteins and host ACE2 receptors predict potential intermediate hosts of SARS-CoV-2. J. Med. Virol. 92, 595–601 (2020).10.1002/jmv.25726 ↗
11. Bouhaddou, M. et al. The global phosphorylation landscape of SARS-CoV-2 infection. Cell 182, 685–712 (2020).10.1016/j.cell.2020.06.034 ↗
12. Fensterl, V. & Sen, G. C. Interferons and viral infections. Biofactors 35, 14–20 (2009).10.1002/biof.6 ↗
13. Haller, O. & Kochs, G. Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity. J. Interf. Cytokine Res. 31, 79–87 (2011).10.1089/jir.2010.0076 ↗
14. Zhou, P. et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 579, 270–273 (2020).10.1038/s41586-020-2012-7 ↗
15. Guo, Y. R. et al. The origin, transmission and clinical therapies on coronavirus disease 2019 (COVID-19) outbreak—an update on the status. Mil. Med. Res. 7, 110 (2020).
16. Letko, M., Marzi, A. & Munster, V. Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses. Nat. Microbiol. 5, 562–569 (2020).10.1038/s41564-020-0688-y ↗
17. Zhang, X. Epidemiology of Covid-19. N. Engl. J. Med. 382, 1869–1869 (2020).10.1056/NEJMc2005157 ↗
18. Ali Hosseini Rad, S. M. & McLellan, A. D. Implications of Sars-Cov-2 mutations for genomic RNA structure and host microRNA targeting. Int. J. Mol. Sci. 21, 1–18 (2020).
19. Sanders, J. M., Monogue, M. L., Jodlowski, T. Z. & Cutrell, J. B. Pharmacologic treatments for coronavirus disease 2019 (COVID-19): a review. J. Am. Med. Assoc. 323, 1824–1836 (2020).10.1001/jama.2019.20153 ↗
20. Tu, Y. et al. A review of SARS-CoV-2 and the ongoing clinical trials. Int. J. Mol. Sci. 21, 2657 (2020).10.3390/ijms21072657 ↗
21. Chong, V. H. et al. Conduction abnormalities in hydroxychloroquine add on therapy to lopinavir/ritonavir in COVID-19. J. Med. Virol. 92, 1–3 (2020).10.1002/jmv.26004 ↗
22. Durante-Mangoni, E. et al. Early experience with remdesivir in SARS-CoV-2 pneumonia. Infection 48, 779–782 (2020).10.1007/s15010-020-01448-x ↗
23. Wang, M. et al. Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-NCoV) in vitro. Cell Res. 30, 269–271 (2020).10.1038/s41422-020-0282-0 ↗
24. Fan, H. H. et al. Repurposing of clinically approved drugs for treatment of coronavirus disease 2019 in a 2019-novel coronavirus-related coronavirus model. Chin. Med. J. 133, 1051–1056 (2020).10.1097/CM9.0000000000000797 ↗
25. Colson, P., Rolain, J. M., Lagier, J. C., Brouqui, P. & Raoult, D. Chloroquine and hydroxychloroquine as available weapons to fight COVID-19. Int. J. Antimicrob. Agents 55, 105932 (2020).10.1016/j.ijantimicag.2020.105932 ↗
26. Sehailia, M. & Chemat, S. Antimalarial-agent artemisinin and derivatives portray more potent binding to Lys353 and Lys31-binding hotspots of SARS-CoV-2 Spike protein than hydroxychloroquine: potential repurposing of artenimol for COVID-19. J. Biomol. Struct. Dyn. https://doi.org/10.1080/07391102.2020.1796809 (2020).10.1080/07391102.2020.1796809 ↗
27. Tan, S. H. S., Hong, C. C., Saha, S., Murphy, D. & Hui, J. H. Medications in COVID-19 patients: summarizing the current literature from an orthopaedic perspective. Int. Orthop. 44, 1599–1603 (2020).10.1007/s00264-020-04643-5 ↗
28. Sodhi, M. & Etminan, M. Therapeutic potential for tetracyclines in the treatment of COVID-19. Pharmacotherapy 40, 487–488 (2020).10.1002/phar.2395 ↗
29. Kuupiel, D. et al. Geographical accessibility to glucose-6-phosphate dioxygenase deficiency point-of-care testing for antenatal care in Ghana. Diagnostics 10, 1–14 (2020).10.3390/diagnostics10040229 ↗
30. Holshue, M. L. et al. First case of 2019 novel coronavirus in the United States. N. Engl. J. Med. 382, 929–936 (2020).10.1056/NEJMoa2001191 ↗
31. Meyerowitz, E. A. et al. Rethinking the role of hydroxychloroquine in the treatment of COVID-19. FASEB J. 34, 6027–6037 (2020).10.1096/fj.202000919 ↗
32. Chouhan, L., Ghimire, S., Subrahmanyam, C., Miyasaka, T. & Biju, V. Synthesis, optoelectronic properties and applications of halide perovskites. Chem. Soc. Rev. 49, 2869 (2020).10.1039/C9CS00848A ↗
33. Biju, V., Itoh, T., Anas, A., Sujith, A. & Ishikawa, M. Semiconductor quantum dots and metal nanoparticles: syntheses, optical properties, and biological applications. Anal. Bioanal. Chem. 391, 2469 (2008).10.1007/s00216-008-2185-7 ↗
34. Biju, V., Itoh, T. & Ishikawa, M. Delivering quantum dots to cells: bioconjugated quantum dots for targeted and nonspecific extracellular and intracellular imaging. Chem. Soc. Rev. 39, 3031 (2010).10.1039/b926512k ↗
35. Usman, K. A. S. et al. Downsizing metal–organic frameworks by bottom-up and topdown methods. NPG Asia Mater. 12, https://doi.org/10.1038/s41427-020-00240-5 (2020).10.1038/s41427-020-00240-5 ↗
36. Murray, C. B., Norris, D. J. & Bawendi, M. G. Synthesis and characterization of nearly monodisperse CdE (E = S, Se, Te) semiconductor nanocrystallites. J. Am. Chem. Soc. 115, 8706 (1993).10.1021/ja00072a025 ↗
37. Biju, V. Chemical modifications and bioconjugate reactions of nanomaterials for sensing, imaging, drug delivery and therapy. Chem. Soc. Rev. 43, 744 (2014).10.1039/C3CS60273G ↗
38. Biju, V. et al. Nanoparticles speckled by ready-to-conjugate lanthanide complexes for multimodal imaging. Nanoscale 7, 14829 (2015).10.1039/C5NR00959F ↗
39. Biju, V. et al. Quantum dot-insect neuropeptide conjugates for fluorescence imaging, transfection, and nucleus targeting of living cells. Langmuir 23, 10254 (2007).10.1021/la7012705 ↗
40. Liong, M. et al. Multifunctional inorganic nanoparticles for imaging, targeting, and drug delivery. ACS Nano 2, 889 (2008).10.1021/nn800072t ↗
41. Dykman, L. & Khlebtsov, N. Gold nanoparticles in biomedical applications: recent advances and perspectives. Chem. Soc. Rev. 41, 2256 (2012).10.1039/C1CS15166E ↗
42. Shibu, E. S. et al. Singlet-oxygen-sensitizing near-infrared-fluorescent multimodal nanoparticles. Angew. Chem. Int. Ed. 52, 10559 (2013).10.1002/anie.201304264 ↗
43. Hell, S. W. & Wichmann, J. Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy. Opt. Lett. 19, 780 (1994).10.1364/OL.19.000780 ↗
44. Kawashima, N., Nakayama, K., Itoh, K., Ishikawa, M. & Biju, V. Reversible dimerization of EGFR revealed by single-molecule fluorescence imaging using quantum dots. Chem. Eur. J. 16, 1186 (2010).10.1002/chem.200902963 ↗
45. Huang, X., El-Sayed, I. H., Qian, W. & El-Sayed, M. A. Cancer cell imaging and photothermal therapy in the near-infrared region by using gold nanorods. J. Am. Chem. Soc. 128, 2115 (2006).10.1021/ja057254a ↗
46. Qian, X. et al. In vivo tumor targeting and spectroscopic detection with surface enhanced raman nanoparticle tags. Nat. Biotechnol. 26, 83 (2008).10.1038/nbt1377 ↗
47. Prompetchara, E., Ketloy, C. & Palaga, T. Immune responses in COVID-19 and potential vaccines: lessons learned from SARS and MERS epidemic. Asian Pac. J. Allergy Immunol. 38, 1 (2020).
48. Ahmed, S. F., Quadeer, A. A. & McKay, M. R. Preliminary identification of potential vaccine targets for the COVID-19 coronavirus (SARS-CoV-2) based on SARS-CoV immunological studies. Viruses 12, https://doi.org/10.3390/v12030254 (2020).10.3390/v12030254 ↗
49. Gurwitz, D. Angiotensin receptor blockers as tentative SARS-CoV-2 therapeutics. Drug Dev. Res. 81, 537 (2020).10.1002/ddr.21656 ↗
50. Tai, W. et al. Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine. Cell. Mol. Immunol. 17, 613 (2020).10.1038/s41423-020-0400-4 ↗
51. Liu, C. et al. Research and development on therapeutic agents and vaccines for COVID-19 and related human coronavirus diseases. ACS Cent. Sci. 6, 315 (2020).10.1021/acscentsci.0c00272 ↗
52. Biju, V. et al. FRET from quantum dots to photodecompose undesired acceptors and report the condensation and decondensation of plasmid DNA. ACS Nano 6, 3776 (2012).10.1021/nn2048608 ↗
53. Anas, A. et al. Clathrin-mediated endocytosis of quantum dot-peptide conjugates in living cells. ACS Nano 3, 2419 (2009).10.1021/nn900663r ↗
54. Biju, V., Mundayoor, S., Omkumar, R. V., Anas, A. & Ishikawa, M. Bioconjugated quantum dots for cancer research: present status, prospects and remaining issues. Biotechnol. Adv. 28, 199 (2010).10.1016/j.biotechadv.2009.11.007 ↗
55. Shibu, E. S. et al. Photouncaging nanoparticles for MRI and fluorescence imaging in vitro and in vivo. ACS Nano 7, 9851 (2013).10.1021/nn4043699 ↗
56. Yuan, Z. et al. Novel fluorinated polycationic delivery of anti-VEGF siRNA for tumor therapy. NPG Asia Mater. 12, https://doi.org/10.1038/s41427-020-0216-9 (2020).10.1038/s41427-020-0216-9 ↗
57. Mu, L. M. et al. Development of functional dendrisomes based on a single molecule of polyesterbenzylether dendrimer and their application in cancer stem cell therapy. NPG Asia Mater. 11, https://doi.org/10.1038/s41427-019-0134-x (2019).10.1038/s41427-019-0134-x ↗
58. Tunesi, M. et al. Hydrogel-based delivery of Tat-fused protein Hsp70 protects dopaminergic cells in vitro and in a mouse model of Parkinson’s disease. NPG Asia Mater. 11, https://doi.org/10.1038/s41427-019-0128-8(2019).10.1038/s41427-019-0128-8 ↗
59. Wang, D., Tai, P. W. L. & Gao, G. Adeno-associated virus vector as a platform for gene therapy delivery. Nat. Rev. Drug Discov. 18, 358 (2019).10.1038/s41573-019-0012-9 ↗
60. Cai, W. et al. Metal–organic framework-based stimuli-responsive systems for drug delivery. Adv. Sci. 6, https://doi.org/10.1002/advs.201801526 (2019).10.1002/advs.201801526 ↗
61. Kauscher, U., Holme, M. N., Björnmalm, M. & Stevens, M. M. Physical stimuli responsive vesicles in drug delivery: beyond liposomes and polymersomes. Adv. Drug Deliv. Rev. 138, 259 (2019).10.1016/j.addr.2018.10.012 ↗
62. Jones, P., Sugino, S., Yamamura, S., Lacy, F. & Biju, V. Impairments of cells and genomic DNA by environmentally transformed engineered nanomaterials. Nanoscale 5, 9511 (2013).10.1039/c3nr03118g ↗
63. Sobhanan, J. et al. Toxicity of nanomaterials due to photochemical degradation and the release of heavy metal ions. Nanoscale. https://doi.org/10.1039/d0nr03957h (2020).10.1039/d0nr03957h ↗
64. Derfus, A. M., Chan, W. C. W. & Bhatia, S. N. Probing the cytotoxicity of semiconductor quantum dots. Nano Lett. 4, 11 (2004).10.1021/nl0347334 ↗
65. Lewinski, N., Colvin, V. & Drezek, R. Cytotoxicity of nanopartides. Small 4, 26 (2008).10.1002/smll.200700595 ↗
66. De Jong, W. H. & Borm, P. J. A. Drug delivery and nanoparticles: applications and hazards. Int. J. Nanomed. 3, 133 (2008).10.2147/IJN.S596 ↗
67. Carr, C. M. & Kim, P. S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823–832 (1993).10.1016/0092-8674(93)90260-W ↗
68. Gallagher, P. E., Ferrario, C. M. & Tallant, E. A. Regulation of ACE2 in cardiac myocytes and fibroblasts. Am. J. Physiol. Heart Circ. Physiol. 295, 2373–2379 (2008).10.1152/ajpheart.00426.2008 ↗
69. Mendoza Torres, E. et al. ACE2 and vasoactive peptides: novel players in cardiovascular/renal remodeling and hypertension. Ther. Adv. Cardiovasc. Dis. 9, 217–237 (2015).10.1177/1753944715597623 ↗
70. Zhou, F. et al. Clinical course and risk factors for mortality of adult inpatients with COVID-19 in Wuhan, China: a retrospective cohort study. Lancet 395, 1054–1062 (2020).10.1016/S0140-6736(20)30566-3 ↗
71. Newburger, J. W. et al. Diagnosis, treatment, and long-term management of Kawasaki disease: a Statement for Health Professionals from the Committee on Rheumatic Fever, Endocarditis and Kawasaki Disease, Council on Cardiovascular Disease in the Young. Am. Heart Assoc. Circ. 110, 2747–2771 (2004).
72. Mourad, J. J. & Levy, B. I. Interaction between RAAS Inhibitors and ACE2 in the context of COVID-19. Nat. Rev. Cardiol. 17, 313 (2020).10.1038/s41569-020-0368-x ↗
73. Zhao, M. Cytokine storm and immunomodulatory therapy in COVID-19: role of chloroquine and anti-IL-6 monoclonal antibodies. Int. J. Antimicrob. Agents 55, 105982 (2020).10.1016/j.ijantimicag.2020.105982 ↗
74. Xu, F. et al. Development of a PH-responsive polymersome inducing endoplasmic reticulum stress and autophagy blockade. Sci. Adv. 6, eabb8725 (2020).10.1126/sciadv.abb8725 ↗
75. Varki, A. Sialic acids in human health and disease. Trends Mol. Med. 14, 351–360 (2008).10.1016/j.molmed.2008.06.002 ↗
76. Paulson, J. C. 5—Interactions of animal viruses with cell surface receptors. Receptors 2, 131–219 (1985).10.1016/B978-0-12-185202-3.50011-1 ↗
77. Sauter, N. K. et al. Binding of influenza virus hemagglutinin to analogs of its cellsurface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography. Biochemistry 31, 9609–9621 (1992).10.1021/bi00155a013 ↗
78. Wasik, B. R., Barnard, K. N. & Parrish, C. R. Effects of sialic acid modifications on virus binding and infection. Trends Microbiol. 24, 991–1001 (2016).10.1016/j.tim.2016.07.005 ↗
79. Wiley, D. C. & Skehel, J. J. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56, 365–394 (1987).10.1146/annurev.bi.56.070187.002053 ↗
80. Carroll, S. M., Higa, H. H. & Paulson, J. C. Different cell-surface receptor determinants of antigenically similar influenza virus hemagglutinins. J. Biol. Chem. 256, 8357–8363 (1981).10.1016/S0021-9258(19)68851-4 ↗
81. Higa, H. H., Rogers, G. N. & Paulson, J. C. Influenza virus hemagglutinins differentiate between receptor determinants bearing N-acetyl-, N-glycollyl-, and N, Odiacetyineuraminic acids. Virology 144, 279–282 (1985).10.1016/0042-6822(85)90325-3 ↗
82. Gagneux, P. et al. Human-specific regulation of Α2-6-linked sialic acids. J. Biol. Chem. 278, 48245–48250 (2003).10.1074/jbc.M309813200 ↗
83. Chen, Y. et al. Human infections with the emerging avian influenza A H7N9 virus from wet market poultry: clinical analysis and characterisation of viral genome. Lancet 381, 1916–1925 (2013).10.1016/S0140-6736(13)60903-4 ↗
84. Weber, P. C., Wendoloski, J. J., Pantoliano, M. W. & Salemme, F. R. Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin. J. Am. Chem. Soc. 114, 3197–3200 (1992).10.1021/ja00035a004 ↗
85. Stayton, P. S. et al. Streptavidin-biotin binding energetics. Biomol. Eng. 16, 39–44 (1999).10.1016/S1050-3862(99)00042-X ↗
86. Chivers, C. E., Koner, A. L., Lowe, E. D. & Howarth, M. How the biotin-streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramer. Biochem. J. 435, 55–63 (2011).10.1042/BJ20101593 ↗
87. Chen, J. et al. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95, 409–417 (1998).10.1016/S0092-8674(00)81771-7 ↗
88. Kruse, H., Goerigk, L. & Grimme, S. Why the standard B3LYP/6-31G* model chemistry should not be used in DFT calculations of molecular thermochemistry: understanding and correcting the problem. J. Org. Chem. 77, 10824–10834 (2012).10.1021/jo302156p ↗
89. Blacklock, B. & Adler, S. A parasite resembling Plasmodium falciparum in a chimpanzee. Ann. Trop. Med. Parasitol. 160, 99–106 (1992).
90. Rodhain, J. Les plasmodium des anthropoids de l’Afrique centrale et leur relation avec les plasmodium humains. Ann. Soc. Belg. Med. Trop. 19, 563–572 (1939).
91. Ollomo, B. et al. Lack of malaria parasite transmission between apes and humans in Gabon. Am. J. Trop. Med. Hyg. 56, 440–445 (1997).10.4269/ajtmh.1997.56.440 ↗
92. Martin, M. J., Rayner, J. C., Gagneux, P., Barnwell, J. W. & Varki, A. Evolution of human–chimpanzee differences in malaria susceptibility: relationship to human genetic loss of N-glycolylneuraminic acid. Proc. Natl Acad. Sci. USA 102, 12819–12824 (2005).10.1073/pnas.0503819102 ↗
93. Escalante, A. A. & Ayala, F. J. Phylogeny of the malarial genus plasmodium, derived from RRNA gene sequences. Proc. Natl Acad. Sci. USA 91, 11373–11377 (1994).10.1073/pnas.91.24.11373 ↗
94. Kalia, M. & Jameel, S. Virus entry paradigms. Amino Acids 41, 1147–1157 (2011).10.1007/s00726-009-0363-3 ↗
95. Klasse, P. J., Bron, R. & Marsh, M. Mechanisms of enveloped virus entry into animal. Cells Adv. Drug Deliv. Rev. 34, 65–91 (1998).10.1016/S0169-409X(98)00002-7 ↗
96. Glebov, O. O. Understanding SARS-CoV-2 endocytosis for COVID-19 drug repurposing. FEBS J. 287, 3664–3671 (2020).10.1111/febs.15369 ↗
97. Celik, O. et al. Combating sars-cov-2 through lipoxins, proteasome, caveolin and nuclear factor-kappa b pathways in non-pregnant and pregnant populations. Cell. Mol. Biol. 66, 221–229 (2020).10.14715/cmb/2020.66.3.36 ↗
98. Gur, M. et al. Conformational transition of SARS-CoV-2 spike glycoprotein between its closed and open states. J. Chem. Phys. 153, 075101 (2020).10.1063/5.0011141 ↗
99. Akira, S., Takeda, K. & Kaisho, T. Toll-like receptors: critical proteins linking innate and acquired immunity. Nat. Immunol. 2, 675–680 (2001).10.1038/90609 ↗
100. Akira, S. & Takeda, K. Toll-like receptor signalling. Nat. Rev. Immunol. 4, 499–511 (2004).10.1038/nri1391 ↗