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A study on the effect of natural products against the transmission of B.1.1.529 Omicron

Alkafaas et al., Virology Journal, doi:10.1186/s12985-023-02160-6

Aug 2023

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Curcumin for COVID-19

15th treatment shown to reduce risk in February 2021

^*, now with p = 0.0000000096 from 27 studies.

Lower risk for mortality, ventilation, hospitalization, progression, recovery, and viral clearance.

No treatment is 100% effective. Protocols combine treatments. ^* >10% efficacy, ≥3 studies.

5,000+ studies for 104 treatments. c19early.org

Review of natural products for SARS-CoV-2 omicron including an In Silico study showing quercetin, curcumin, ascorbic acid, nigellidine, and chloroquine among many compounds docked to the ACE2 metallopeptidase domain. Quercetin, curcumin, and ascorbic acid bound ACE2 with energy scores of -16.51, -13.5, and -12.55 kcal/mol. Nigellidine and chloroquine bound with lower affinity (-11.73 and -10.33 kcal/mol). The results suggest these compounds may have potential to inhibit SARS-CoV-2 infection by binding the ACE2 receptor.

47 preclinical studies support the efficacy of curcumin for COVID-19:

24 In Silico studies1-24

22 In Vitro studies1,5,7,11,17,21,25-40

1 In Vivo animal study5

In Silico studies predict inhibition of SARS-CoV-2 with curcumin or metabolites via binding to the spikeA,5,10,12,18,21 (and specifically the receptor binding domainB,8,11,14), M^proC,5,7,9-11,13,14,16,19,21,22,24,37, RNA-dependent RNA polymeraseD,11,20, ACE2E,12,13,15, nucleocapsidF,6,23, nsp10G,23, and helicaseH,27 proteins. In Vitro studies demonstrate inhibition of the spikeA,32 (and specifically the receptor binding domainB,40), M^proC,17,32,37,39, ACE2E,40, and TMPRSS2I,40 proteins, and inhibition of spike-ACE2 interactionJ,25. In Vitro studies demonstrate efficacy in Calu-3K,38, A549L,32, 293TM,1, HEK293-hACE2N,17,30, 293T/hACE2/TMPRSS2O,31, Vero E6P,7,11,21,30,32-34,36,38, and SH-SY5YQ,29 cells. Curcumin is predicted to inhibit the interaction between the SARS-CoV-2 spike protein receptor binding domain and the human ACE2 receptor for the delta and omicron variants8, decreases pro-inflammatory cytokines induced by SARS-CoV-2 in peripheral blood mononuclear cells36, alleviates SARS-CoV-2 spike protein-induced mitochondrial membrane damage and oxidative stress1, and may limit COVID-19 induced cardiac damage by inhibiting the NF-κB signaling pathway which mediates the profibrotic effects of the SARS-CoV-2 spike protein on cardiac fibroblasts41.

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Study covers quercetin, curcumin, nigella sativa, vitamin C, and HCQ.

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2. Öztürkkan et al., In Silico investigation of the effects of curcuminoids on the spike protein of the omicron variant of SARS-CoV-2, Baku State University Journal of Chemistry and Material Sciences, 1:2, bsuj.bsu.edu.az/uploads/pdf/ec4204d62f7802de54e6092bf7860029.pdf.edu.az.

3. Yunze et al., Therapeutic effect and potential mechanism of curcumin, an active ingredient in Tongnao Decoction, on COVID-19 combined with stroke: a network pharmacology study and GEO database mining, Research Square, doi:10.21203/rs.3.rs-4329762/v1.researchsquare.com, doi.org.

4. Agamah et al., Network-based multi-omics-disease-drug associations reveal drug repurposing candidates for COVID-19 disease phases, ScienceOpen, doi:10.58647/DRUGARXIV.PR000010.v1.scienceopen.com, doi.org.

5. Boseila et al., Throat spray formulated with virucidal Pharmaceutical excipients as an effective early prophylactic or treatment strategy against pharyngitis post-exposure to SARS CoV-2, European Journal of Pharmaceutics and Biopharmaceutics, doi:10.1016/j.ejpb.2024.114279.sciencedirect.com, doi.org.

6. Hidayah et al., Bioinformatics study of curcumin, demethoxycurcumin, bisdemethoxycurcumin and cyclocurcumin compounds in Curcuma longa as an antiviral agent via nucleocapsid on SARS-CoV-2 inhibition, International Conference on Organic and Applied Chemistry, doi:10.1063/5.0197724.aip.org, doi.org.

7. Singh et al., Unlocking the potential of phytochemicals in inhibiting SARS-CoV-2 M Pro protein - An in-silico and cell-based approach, Research Square, doi:10.21203/rs.3.rs-3888947/v1.researchsquare.com, doi.org.

8. Kant et al., Structure-based drug discovery to identify SARS-CoV2 spike protein–ACE2 interaction inhibitors, Journal of Biomolecular Structure and Dynamics, doi:10.1080/07391102.2023.2300060.tandfonline.com, doi.org.

9. Naderi Beni et al., In silico studies of anti-oxidative and hot temperament-based phytochemicals as natural inhibitors of SARS-CoV-2 Mpro, PLOS ONE, doi:10.1371/journal.pone.0295014.plos.org, doi.org.

10. Moschovou et al., Exploring the Binding Effects of Natural Products and Antihypertensive Drugs on SARS-CoV-2: An In Silico Investigation of Main Protease and Spike Protein, International Journal of Molecular Sciences, doi:10.3390/ijms242115894.mdpi.com, doi.org.

11. Eleraky et al., Curcumin Transferosome-Loaded Thermosensitive Intranasal in situ Gel as Prospective Antiviral Therapy for SARS-Cov-2, International Journal of Nanomedicine, doi:10.2147/IJN.S423251.dovepress.com, doi.org.

12. Singh (B) et al., Computational studies to analyze effect of curcumin inhibition on coronavirus D614G mutated spike protein, The Seybold Report, doi:10.17605/OSF.IO/TKEXJ.ac.in, doi.org.

13. Thapa et al., In-silico Approach for Predicting the Inhibitory Effect of Home Remedies on Severe Acute Respiratory Syndrome Coronavirus-2, Makara Journal of Science, doi:10.7454/mss.v27i3.1609.ac.id, doi.org.

14. Srivastava et al., Paradigm of Well-Orchestrated Pharmacokinetic Properties of Curcuminoids Relative to Conventional Drugs for the Inactivation of SARS-CoV-2 Receptors: An In Silico Approach, Stresses, doi:10.3390/stresses3030043.mdpi.com, doi.org.

15. Alkafaas et al., A study on the effect of natural products against the transmission of B.1.1.529 Omicron, Virology Journal, doi:10.1186/s12985-023-02160-6.biomedcentral.com, doi.org.

16. Winih Kinasih et al., Analisis in silico interaksi senyawa kurkuminoid terhadap enzim main protease 6LU7 dari SARS-CoV-2, Duta Pharma Journal, doi:10.47701/djp.v3i1.2904.ac.id, doi.org.

17. Wu et al., Potential Mechanism of Curcumin and Resveratrol against SARS-CoV-2, Research Square, doi:10.21203/rs.3.rs-2780614/v1.researchsquare.com, doi.org.

18. Nag et al., Curcumin inhibits spike protein of new SARS-CoV-2 variant of concern (VOC) Omicron, an in silico study, Computers in Biology and Medicine, doi:10.1016/j.compbiomed.2022.105552.sciencedirect.com, doi.org.

19. Rampogu et al., Molecular Docking and Molecular Dynamics Simulations Discover Curcumin Analogue as a Plausible Dual Inhibitor for SARS-CoV-2, International Journal of Molecular Sciences, doi:10.3390/ijms23031771.mdpi.com, doi.org.

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21. Kandeil et al., Bioactive Polyphenolic Compounds Showing Strong Antiviral Activities against Severe Acute Respiratory Syndrome Coronavirus 2, Pathogens, doi:10.3390/pathogens10060758.mdpi.com, doi.org.

22. Rajagopal et al., Activity of phytochemical constituents of Curcuma longa (turmeric) and Andrographis paniculata against coronavirus (COVID-19): an in silico approach, Future Journal of Pharmaceutical Sciences, doi:10.1186/s43094-020-00126-x.springeropen.com, doi.org.

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24. Sekiou et al., In-Silico Identification of Potent Inhibitors of COVID-19 Main Protease (Mpro) and Angiotensin Converting Enzyme 2 (ACE2) from Natural Products: Quercetin, Hispidulin, and Cirsimaritin Exhibited Better Potential Inhibition than Hydroxy-Chloroquine Against COVID-19 Main Protease Active Site and ACE2, ChemRxiv, doi:10.26434/chemrxiv.12181404.v1.chemrxiv.org, doi.org.

25. Emam et al., Establishment of in-house assay for screening of anti-SARS-CoV-2 protein inhibitors, AMB Express, doi:10.1186/s13568-024-01739-8.springeropen.com, doi.org.

26. Van Tin et al., Spike Protein of SARS-CoV-2 Activates Cardiac Fibrogenesis through NLRP3 Inflammasomes and NF-κB Signaling, Cells, doi:10.3390/cells13161331.mdpi.com, doi.org.

27. Li et al., Thermal shift assay (TSA)-based drug screening strategy for rapid discovery of inhibitors against the Nsp13 helicase of SARS-CoV-2, Animals and Zoonoses, doi:10.1016/j.azn.2024.06.001.sciencedirect.com, doi.org.

28. Kamble et al., Nanoparticulate curcumin spray imparts prophylactic and therapeutic properties against SARS-CoV-2, Emergent Materials, doi:10.1007/s42247-024-00754-6.springer.com, doi.org.

29. Nicoliche et al., Antiviral, anti-inflammatory and antioxidant effects of curcumin and curcuminoids in SH-SY5Y cells infected by SARS-CoV-2, Scientific Reports, doi:10.1038/s41598-024-61662-7.nature.com, doi.org.

30. Nittayananta et al., A novel film spray containing curcumin inhibits SARS-CoV-2 and influenza virus infection and enhances mucosal immunity, Virology Journal, doi:10.1186/s12985-023-02282-x.biomedcentral.com, doi.org.

31. Septisetyani et al., Curcumin and turmeric extract inhibited SARS-CoV-2 pseudovirus cell entry and Spike mediated cell fusion, bioRxiv, doi:10.1101/2023.09.28.560070.biorxiv.org, doi.org.

32. Mohd Abd Razak et al., In Vitro Anti-SARS-CoV-2 Activities of Curcumin and Selected Phenolic Compounds, Natural Product Communications, doi:10.1177/1934578X231188861.sagepub.com, doi.org.

33. Teshima et al., Antiviral activity of curcumin and its analogs selected by an artificial intelligence-supported activity prediction system in SARS-CoV-2-infected VeroE6 cells, Natural Product Research, doi:10.1080/14786419.2023.2194647.tandfonline.com, doi.org.

34. Leka et al., In vitro antiviral activity against SARS-CoV-2 of common herbal medicinal extracts and their bioactive compounds, Phytotherapy Research, doi:10.1002/ptr.7463.wiley.com, doi.org.

35. Goc et al., Inhibitory effects of specific combination of natural compounds against SARS-CoV-2 and its Alpha, Beta, Gamma, Delta, Kappa, and Mu variants, European Journal of Microbiology and Immunology, doi:10.1556/1886.2021.00022.akjournals.com, doi.org.

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40. Goc (B) et al., Phenolic compounds disrupt spike-mediated receptor-binding and entry of SARS-CoV-2 pseudo-virions, PLOS ONE, doi:10.1371/journal.pone.0253489.plos.org, doi.org.

41. Van Tin (B) et al., Spike Protein of SARS-CoV-2 Activates Cardiac Fibrogenesis through NLRP3 Inflammasomes and NF-κB Signaling, Cells, doi:10.3390/cells13161331.mdpi.com, doi.org.

a. The trimeric spike (S) protein is a glycoprotein that mediates viral entry by binding to the host ACE2 receptor, is critical for SARS-CoV-2's ability to infect host cells, and is a target of neutralizing antibodies. Inhibition of the spike protein prevents viral attachment, halting infection at the earliest stage.

b. The receptor binding domain is a specific region of the spike protein that binds ACE2 and is a major target of neutralizing antibodies. Focusing on the precise binding site allows highly specific disruption of viral attachment with reduced potential for off-target effects.

c. The main protease or M^pro, also known as 3CL^pro or nsp5, is a cysteine protease that cleaves viral polyproteins into functional units needed for replication. Inhibiting M^pro disrupts the SARS-CoV-2 lifecycle within the host cell, preventing the creation of new copies.

d. RNA-dependent RNA polymerase (RdRp), also called nsp12, is the core enzyme of the viral replicase-transcriptase complex that copies the positive-sense viral RNA genome into negative-sense templates for progeny RNA synthesis. Inhibiting RdRp blocks viral genome replication and transcription.

e. The angiotensin converting enzyme 2 (ACE2) protein is a host cell transmembrane protein that serves as the cellular receptor for the SARS-CoV-2 spike protein. ACE2 is expressed on many cell types, including epithelial cells in the lungs, and allows the virus to enter and infect host cells. Inhibition may affect ACE2's physiological function in blood pressure control.

f. The nucleocapsid (N) protein binds and encapsulates the viral genome by coating the viral RNA. N enables formation and release of infectious virions and plays additional roles in viral replication and pathogenesis. N is also an immunodominant antigen used in diagnostic assays.

g. Non-structural protein 10 (nsp10) serves as an RNA chaperone and stabilizes conformations of nsp12 and nsp14 in the replicase-transcriptase complex, which synthesizes new viral RNAs. Nsp10 disruption may destabilize replicase-transcriptase complex activity.

h. The helicase, or nsp13, protein unwinds the double-stranded viral RNA, a crucial step in replication and transcription. Inhibition may prevent viral genome replication and the creation of new virus components.

i. Transmembrane protease serine 2 (TMPRSS2) is a host cell protease that primes the spike protein, facilitating cellular entry. TMPRSS2 activity helps enable cleavage of the spike protein required for membrane fusion and virus entry. Inhibition may especially protect respiratory epithelial cells, buy may have physiological effects.

j. The interaction between the SARS-CoV-2 spike protein and the human ACE2 receptor is a primary method of viral entry, inhibiting this interaction can prevent the virus from attaching to and entering host cells, halting infection at an early stage.

k. Calu-3 is a human lung adenocarcinoma cell line with moderate ACE2 and TMPRSS2 expression and SARS-CoV-2 susceptibility. It provides a model of the human respiratory epithelium, but many not be ideal for modeling early stages of infection due to the moderate expression levels of ACE2 and TMPRSS2.

l. A549 is a human lung carcinoma cell line with low ACE2 expression and SARS-CoV-2 susceptibility. Viral entry/replication can be studied but the cells may not replicate all aspects of lung infection.

m. 293T is a human embryonic kidney cell line that can be engineered for high ACE2 expression and SARS-CoV-2 susceptibility. 293T cells are easily transfected and support high protein expression.

n. HEK293-hACE2 is a human embryonic kidney cell line with high ACE2 expression and SARS-CoV-2 susceptibility. Cells have been transfected with a plasmid to express the human ACE2 (hACE2) protein.

o. 293T/hACE2/TMPRSS2 is a human embryonic kidney cell line engineered for high ACE2 and TMPRSS2 expression, which mimics key aspects of human infection. 293T/hACE2/TMPRSS2 cells are very susceptible to SARS-CoV-2 infection.

p. Vero E6 is an African green monkey kidney cell line with low/no ACE2 expression and high SARS-CoV-2 susceptibility. The cell line is easy to maintain and supports robust viral replication, however the monkey origin may not accurately represent human responses.

q. SH-SY5Y is a human neuroblastoma cell line that exhibits neuronal phenotypes. It is commonly used as an in vitro model for studying neurotoxicity, neurodegenerative diseases, and neuronal differentiation.

Alkafaas et al., 25 Aug 2023, peer-reviewed, 12 authors. Contact: samar.alkafas@science.tanta.edu.eg, samarsamy2017@yahoo.com, ghoshs@ufs.ac.za, soumyaghosh@yahoo.com, h.onyeaka@bham.ac.uk.

In Silico studies are an important part of preclinical research, however results may be very different in vivo.

This Paper Curcumin All

A study on the effect of natural products against the transmission of B.1.1.529 Omicron

Samar Sami Alkafaas, Abanoub Mosaad Abdallah, Aya Misbah Hussien, Heba Bedair, Mahmoud Abdo, Soumya Ghosh, Sara Samy Elkafas, Wilgince Apollon, Morteza Saki, Samah A Loutfy, Helen Onyeaka, Mohamed Hessien

Virology Journal, doi:10.1186/s12985-023-02160-6

Background The recent outbreak of the Coronavirus pandemic resulted in a successful vaccination program launched by the World Health Organization. However, a large population is still unvaccinated, leading to the emergence of mutated strains like alpha, beta, delta, and B.1.1.529 (Omicron). Recent reports from the World Health Organization raised concerns about the Omicron variant, which emerged in South Africa during a surge in COVID-19 cases in November 2021. Vaccines are not proven completely effective or safe against Omicron, leading to clinical trials for combating infection by the mutated virus. The absence of suitable pharmaceuticals has led scientists and clinicians to search for alternative and supplementary therapies, including dietary patterns, to reduce the effect of mutated strains. Main body This review analyzed Coronavirus aetiology, epidemiology, and natural products for combating Omicron. Although the literature search did not include keywords related to in silico or computational research, in silico investigations were emphasized in this study. Molecular docking was implemented to compare the interaction between natural products and Chloroquine with the ACE2 receptor protein amino acid residues of Omicron. The global Omicron infection proceeding SARS-CoV-2 vaccination was also elucidated. The docking results suggest that DGCG may bind to the ACE2 receptor three times more effectively than standard chloroquine. Conclusion The emergence of the Omicron variant has highlighted the need for alternative therapies to reduce the impact of mutated strains. The current review suggests that natural products such as DGCG may be effective in binding to the ACE2 receptor and combating the Omicron variant, however, further research is required to validate the results of this study and explore the potential of natural products to mitigate COVID-19. Highlights • There are 32 mutations in the spike of the Omicron variant. • Non-SARS-COV-2 vaccinated individuals accelerate transmission of Omicron variant.

Declarations Ethics approval and consent to participate Not applicable. Consent for publication All the authors read and agreed to publish this article. Competing interests The authors declare that they have no competing interests. Publisher's Note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

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{ 'indexed': {'date-parts': [[2024, 2, 6]], 'date-time': '2024-02-06T18:28:03Z', 'timestamp': 1707244083411}, 'reference-count': 221, 'publisher': 'Springer Science and Business Media LLC', 'issue': '1', 'license': [ { 'start': { 'date-parts': [[2023, 8, 25]], 'date-time': '2023-08-25T00:00:00Z', 'timestamp': 1692921600000}, 'content-version': 'tdm', 'delay-in-days': 0, 'URL': 'https://creativecommons.org/licenses/by/4.0'}, { 'start': { 'date-parts': [[2023, 8, 25]], 'date-time': '2023-08-25T00:00:00Z', 'timestamp': 1692921600000}, 'content-version': 'vor', 'delay-in-days': 0, 'URL': 'https://creativecommons.org/licenses/by/4.0'}], 'funder': [ { 'name': 'The Science, Technology & Innovation Funding Authority (STDF) in cooperation with ' 'the Egyptian Knowledge Bank'}, {'DOI': '10.13039/501100007950', 'name': 'Tanta University', 'doi-asserted-by': 'crossref'}], 'content-domain': {'domain': ['link.springer.com'], 'crossmark-restriction': False}, 'abstract': 'Abstract\n' ' Background\n' ' The recent outbreak of the Coronavirus pandemic resulted in a ' 'successful vaccination program launched by the World Health Organization. However, a large ' 'population is still unvaccinated, leading to the emergence of mutated strains like alpha, ' 'beta, delta, and B.1.1.529 (Omicron). Recent reports from the World Health Organization ' 'raised concerns about the Omicron variant, which emerged in South Africa during a surge in ' 'COVID-19 cases in November 2021. Vaccines are not proven completely effective or safe against ' 'Omicron, leading to clinical trials for combating infection by the mutated virus. The absence ' 'of suitable pharmaceuticals has led scientists and clinicians to search for alternative and ' 'supplementary therapies, including dietary patterns, to reduce the effect of mutated ' 'strains.\n' ' \n' ' Main body\n' ' This review analyzed Coronavirus aetiology, epidemiology, and natural ' 'products for combating Omicron. Although the literature search did not include keywords ' 'related to in silico or computational research, in silico investigations were emphasized in ' 'this study. Molecular docking was implemented to compare the interaction between natural ' 'products and Chloroquine with the ACE2 receptor protein amino acid residues of Omicron. The ' 'global Omicron infection proceeding SARS-CoV-2 vaccination was also elucidated. The docking ' 'results suggest that DGCG may bind to the ACE2 receptor three times more effectively than ' 'standard chloroquine.\n' ' \n' ' Conclusion\n' ' The emergence of the Omicron variant has highlighted the need for ' 'alternative therapies to reduce the impact of mutated strains. The current review suggests ' 'that natural products such as DGCG may be effective in binding to the ACE2 receptor and ' 'combating the Omicron variant, however, further research is required to validate the results ' 'of this study and explore the potential of natural products to mitigate COVID-19.\n' ' \n' ' Graphical abstract\n' ' \n' ' ', 'DOI': '10.1186/s12985-023-02160-6', 'type': 'journal-article', 'created': {'date-parts': [[2023, 8, 25]], 'date-time': '2023-08-25T06:02:14Z', 'timestamp': 1692943334000}, 'update-policy': 'http://dx.doi.org/10.1007/springer_crossmark_policy', 'source': 'Crossref', 'is-referenced-by-count': 3, 'title': 'A study on the effect of natural products against the transmission of B.1.1.529 Omicron', 'prefix': '10.1186', 'volume': '20', 'author': [ {'given': 'Samar Sami', 'family': 'Alkafaas', 'sequence': 'first', 'affiliation': []}, {'given': 'Abanoub Mosaad', 'family': 'Abdallah', 'sequence': 'additional', 'affiliation': []}, {'given': 'Aya Misbah', 'family': 'Hussien', 'sequence': 'additional', 'affiliation': []}, {'given': 'Heba', 'family': 'Bedair', 'sequence': 'additional', 'affiliation': []}, {'given': 'Mahmoud', 'family': 'Abdo', 'sequence': 'additional', 'affiliation': []}, {'given': 'Soumya', 'family': 'Ghosh', 'sequence': 'additional', 'affiliation': []}, {'given': 'Sara Samy', 'family': 'Elkafas', 'sequence': 'additional', 'affiliation': []}, {'given': 'Wilgince', 'family': 'Apollon', 'sequence': 'additional', 'affiliation': []}, {'given': 'Morteza', 'family': 'Saki', 'sequence': 'additional', 'affiliation': []}, {'given': 'Samah A.', 'family': 'Loutfy', 'sequence': 'additional', 'affiliation': []}, {'given': 'Helen', 'family': 'Onyeaka', 'sequence': 'additional', 'affiliation': []}, {'given': 'Mohamed', 'family': 'Hessien', 'sequence': 'additional', 'affiliation': []}], 'member': '297', 'published-online': {'date-parts': [[2023, 8, 25]]}, 'reference': [ { 'key': '2160_CR1', 'doi-asserted-by': 'crossref', 'first-page': '1', 'DOI': '10.12998/wjcc.v10.i1.1', 'volume': '10', 'author': 'S-Y Ren', 'year': '2022', 'unstructured': 'Ren S-Y, Wang W-B, Gao R-D, Zhou A-M. 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Clin Pract. 2020;10:24–30.', 'journal-title': 'Clin Pract'}, { 'key': '2160_CR204', 'doi-asserted-by': 'crossref', 'first-page': '540', 'DOI': '10.3390/antiox9060540', 'volume': '9', 'author': 'FA Wagener', 'year': '2020', 'unstructured': 'Wagener FA, Pickkers P, Peterson SJ, Immenschuh S, Abraham NG. Targeting ' 'the heme-heme oxygenase system to prevent severe complications following ' 'COVID-19 infections. Antioxidants. 2020;9:540.', 'journal-title': 'Antioxidants'}, { 'key': '2160_CR205', 'first-page': 'e00127', 'volume': '94', 'author': 'Y Wan', 'year': '2020', 'unstructured': 'Wan Y, Shang J, Graham R, Baric RS, Li F. Receptor recognition by the ' 'novel coronavirus from Wuhan: an analysis based on decade-long ' 'structural studies of SARS coronavirus. J Virol. 2020;94:e00127-e1120.', 'journal-title': 'J Virol'}, { 'key': '2160_CR206', 'doi-asserted-by': 'crossref', 'first-page': '1444', 'DOI': '10.1126/science.abb2762', 'volume': '367', 'author': 'R Yan', 'year': '2020', 'unstructured': 'Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q. Structural basis for the ' 'recognition of SARS-CoV-2 by full-length human ACE2. Science. ' '2020;367:1444–8.', 'journal-title': 'Science'}, { 'key': '2160_CR207', 'doi-asserted-by': 'crossref', 'first-page': '473', 'DOI': '10.1126/science.abb8925', 'volume': '368', 'author': 'JB Moore', 'year': '2020', 'unstructured': 'Moore JB, June CH. Cytokine release syndrome in severe COVID-19. ' 'Science. 2020;368:473–4.', 'journal-title': 'Science'}, { 'key': '2160_CR208', 'doi-asserted-by': 'crossref', 'first-page': '105960', 'DOI': '10.1016/j.ijantimicag.2020.105960', 'volume': '55', 'author': 'J Fantini', 'year': '2020', 'unstructured': 'Fantini J, Di Scala C, Chahinian H, Yahi N. Structural and molecular ' 'modelling studies reveal a new mechanism of action of chloroquine and ' 'hydroxychloroquine against SARS-CoV-2 infection. Int J Antimicrob ' 'Agents. 2020;55:105960.', 'journal-title': 'Int J Antimicrob Agents'}, { 'key': '2160_CR209', 'unstructured': 'MOE V: Chemical Computing Group Inc., Montreal, Canada. 2010.'}, { 'key': '2160_CR210', 'doi-asserted-by': 'crossref', 'first-page': '136301', 'DOI': '10.1016/j.molstruc.2023.136301', 'volume': '1292', 'author': 'AM Abdallah', 'year': '2023', 'unstructured': 'Abdallah AM, Gomha SM, Zaki MEA, Abolibda TZ, Kheder NA. A green ' 'synthesis, DFT calculations, and molecular docking study of some new ' 'indeno[2,1-b]quinoxalines containing thiazole moiety. J Mol Struct. ' '2023;1292:136044.', 'journal-title': 'J Mol Struct'}, { 'key': '2160_CR211', 'doi-asserted-by': 'crossref', 'unstructured': 'Al-Qaisi ZH, Al-Garawi ZS, Al-Karawi AJM, Hammood AJ, Abdallah AM, Clegg ' 'W, Mohamed GG. Antiureolytic activity of new water-soluble thiadiazole ' 'derivatives: Spectroscopic, DFT, and molecular docking studies. ' 'Spectrochim Acta A Mol Biomol Spectrosc. 2022;272:120971.', 'DOI': '10.1016/j.saa.2022.120971'}, { 'key': '2160_CR212', 'doi-asserted-by': 'crossref', 'unstructured': 'Abubakar MB, Usman D, El-Saber Batiha G, Cruz-Martins N, Malami I, ' 'Ibrahim KG, Abubakar B, Bello MB, Muhammad A, Gan SH, Dabai AI, Alblihed ' 'M, Ghosh A, Badr RH, Thangadurai D, Imam MU. Natural Products Modulating ' 'Angiotensin Converting Enzyme 2 (ACE2) as Potential COVID-19 Therapies. ' 'Front Pharmacol. 2021;12:629935.', 'DOI': '10.3389/fphar.2021.629935'}, { 'key': '2160_CR213', 'doi-asserted-by': 'crossref', 'first-page': '55', 'DOI': '10.1007/s40203-021-00114-w', 'volume': '9', 'author': 'MF Isaac-Lam', 'year': '2021', 'unstructured': 'Isaac-Lam MF. Molecular modeling of the interaction of ligands with ' 'ACE2–SARS-CoV-2 spike protein complex. In Silico Pharmacol. 2021;9:55.', 'journal-title': 'In Silico Pharmacol'}, { 'key': '2160_CR214', 'doi-asserted-by': 'crossref', 'unstructured': 'Wasilewicz A, Kirchweger B, Bojkova D, Abi Saad MJ, Langeder J, ' 'Bütikofer M, Adelsberger S, Grienke U, Cinatl J Jr, Petermann O, ' 'Scapozza L, Orts J, Kirchmair J, Rabenau HF, Rollinger JM. ' 'Identification of Natural Products Inhibiting SARS-CoV-2 by Targeting ' 'Viral Proteases: A Combined in Silico and in Vitro Approach. J Nat Prod. ' '2023;86(2):264-275.', 'DOI': '10.1021/acs.jnatprod.2c00843'}, { 'key': '2160_CR215', 'doi-asserted-by': 'crossref', 'first-page': '105155', 'DOI': '10.1016/j.compbiomed.2021.105155', 'volume': '141', 'author': 'MBS Al-Shuhaib', 'year': '2022', 'unstructured': 'Al-Shuhaib MBS, Hashim HO, Al-Shuhaib JM. Epicatechin is a promising ' 'novel inhibitor of SARS-CoV-2 entry by disrupting interactions between ' 'angiotensin-converting enzyme type 2 and the viral receptor binding ' 'domain: a computational/simulation study. Comput Biol Med. ' '2022;141:105155.', 'journal-title': 'Comput Biol Med'}, { 'key': '2160_CR216', 'doi-asserted-by': 'crossref', 'unstructured': 'Mohammadi Pour P, Fakhri S, Asgary S, Farzaei MH, Echeverría J. The ' 'signaling pathways, and therapeutic targets of antiviral agents: ' 'focusing on the antiviral approaches and clinical perspectives of ' 'anthocyanins in the management of viral diseases. Front Pharmacol. ' '2019;1207.', 'DOI': '10.3389/fphar.2019.01207'}, { 'key': '2160_CR217', 'first-page': '209', 'volume': '45', 'author': 'Y Knox', 'year': '2001', 'unstructured': 'Knox Y, Hayashi K, Suzutani T, Ogasawara M, Yoshida I, Shiina R, Tsukui ' 'A, Terahara N, Azuma M. Activity of anthocyanins from fruit extract of ' 'Ribes nigrum L. against influenza A and B viruses. Acta virol. ' '2001;45:209–15.', 'journal-title': 'Acta virol'}, { 'key': '2160_CR218', 'doi-asserted-by': 'crossref', 'first-page': '2066', 'DOI': '10.3390/molecules23082066', 'volume': '23', 'author': 'A Di Sotto', 'year': '2018', 'unstructured': 'Di Sotto A, Di Giacomo S, Amatore D, Locatelli M, Vitalone A, Toniolo C, ' 'Rotino GL, Lo Scalzo R, Palamara AT, Marcocci ME. A polyphenol rich ' 'extract from Solanum melongena L. DR2 peel exhibits antioxidant ' 'properties and anti-herpes simplex virus type 1 activity in vitro. ' 'Molecules. 2018;23:2066.', 'journal-title': 'Molecules'}, { 'key': '2160_CR219', 'doi-asserted-by': 'crossref', 'first-page': '1314', 'DOI': '10.3389/fmicb.2017.01314', 'volume': '8', 'author': 'Á Vázquez-Calvo', 'year': '2017', 'unstructured': 'Vázquez-Calvo Á, Jiménez De Oya N, Martín-Acebes MA, Garcia-Moruno E, ' 'Saiz J-C. Antiviral properties of the natural polyphenols delphinidin ' 'and epigallocatechin gallate against the flaviviruses West Nile virus, ' 'Zika virus, and dengue virus. Front Microbiol. 2017;8:1314.', 'journal-title': 'Front Microbiol'}, { 'key': '2160_CR220', 'doi-asserted-by': 'crossref', 'first-page': '10053', 'DOI': '10.1128/JVI.01473-15', 'volume': '89', 'author': 'N Calland', 'year': '2015', 'unstructured': 'Calland N, Sahuc M-E, Belouzard S, Pène V, Bonnafous P, Mesalam AA, ' 'Deloison G, Descamps V, Sahpaz S, Wychowski C. Polyphenols inhibit ' 'hepatitis C virus entry by a new mechanism of action. J Virol. ' '2015;89:10053–63.', 'journal-title': 'J Virol'}, { 'key': '2160_CR221', 'doi-asserted-by': 'crossref', 'first-page': '6563', 'DOI': '10.1007/s00216-013-7068-x', 'volume': '405', 'author': 'K Swaminathan', 'year': '2013', 'unstructured': 'Swaminathan K, Dyason JC, Maggioni A, von Itzstein M, Downard KM. ' 'Binding of a natural anthocyanin inhibitor to influenza neuraminidase by ' 'mass spectrometry. Anal Bioanal Chem. 2013;405:6563–72.', 'journal-title': 'Anal Bioanal Chem'}], 'container-title': 'Virology Journal', 'original-title': [], 'language': 'en', 'link': [ { 'URL': 'https://link.springer.com/content/pdf/10.1186/s12985-023-02160-6.pdf', 'content-type': 'application/pdf', 'content-version': 'vor', 'intended-application': 'text-mining'}, { 'URL': 'https://link.springer.com/article/10.1186/s12985-023-02160-6/fulltext.html', 'content-type': 'text/html', 'content-version': 'vor', 'intended-application': 'text-mining'}, { 'URL': 'https://link.springer.com/content/pdf/10.1186/s12985-023-02160-6.pdf', 'content-type': 'application/pdf', 'content-version': 'vor', 'intended-application': 'similarity-checking'}], 'deposited': { 'date-parts': [[2023, 11, 18]], 'date-time': '2023-11-18T22:18:41Z', 'timestamp': 1700345921000}, 'score': 1, 'resource': {'primary': {'URL': 'https://virologyj.biomedcentral.com/articles/10.1186/s12985-023-02160-6'}}, 'subtitle': [], 'short-title': [], 'issued': {'date-parts': [[2023, 8, 25]]}, 'references-count': 221, 'journal-issue': {'issue': '1', 'published-online': {'date-parts': [[2023, 12]]}}, 'alternative-id': ['2160'], 'URL': 'http://dx.doi.org/10.1186/s12985-023-02160-6', 'relation': {}, 'ISSN': ['1743-422X'], 'subject': ['Infectious Diseases', 'Virology'], 'container-title-short': 'Virol J', 'published': {'date-parts': [[2023, 8, 25]]}, 'assertion': [ { 'value': '29 March 2023', 'order': 1, 'name': 'received', 'label': 'Received', 'group': {'name': 'ArticleHistory', 'label': 'Article History'}}, { 'value': '15 August 2023', 'order': 2, 'name': 'accepted', 'label': 'Accepted', 'group': {'name': 'ArticleHistory', 'label': 'Article History'}}, { 'value': '25 August 2023', 'order': 3, 'name': 'first_online', 'label': 'First Online', 'group': {'name': 'ArticleHistory', 'label': 'Article History'}}, {'order': 1, 'name': 'Ethics', 'group': {'name': 'EthicsHeading', 'label': 'Declarations'}}, { 'value': 'Not applicable.', 'order': 2, 'name': 'Ethics', 'group': {'name': 'EthicsHeading', 'label': 'Ethics approval and consent to participate'}}, { 'value': 'All the authors read and agreed to publish this article.', 'order': 3, 'name': 'Ethics', 'group': {'name': 'EthicsHeading', 'label': 'Consent for publication'}}, { 'value': 'The authors declare that they have no competing interests.', 'order': 4, 'name': 'Ethics', 'group': {'name': 'EthicsHeading', 'label': 'Competing interests'}}], 'article-number': '191'}

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