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All Studies   Meta Analysis    Recent:   

Exploring the binding efficacy of ivermectin against the key proteins of SARS-CoV-2 pathogenesis: an in silico approach

Choudhury et al., Future Medicine, doi:10.2217/fvl-2020-0342
Mar 2021  
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Ivermectin for COVID-19
4th treatment shown to reduce risk in August 2020
 
*, now with p < 0.00000000001 from 104 studies, recognized in 22 countries.
No treatment is 100% effective. Protocols combine treatments. * >10% efficacy, ≥3 studies.
4,300+ studies for 75 treatments. c19ivm.org
In Silico analysis finding that ivermectin has high binding affinity for the SARS-CoV-2 viral spike protein, main protease, replicase, and human TMPRSS2 receptors.
68 preclinical studies support the efficacy of ivermectin for COVID-19:
Ivermectin, better known for antiparasitic activity, is a broad spectrum antiviral with activity against many viruses including H7N766, Dengue32,67,68, HIV-168, Simian virus 4069, Zika32,70,71, West Nile71, Yellow Fever72,73, Japanese encephalitis72, Chikungunya73, Semliki Forest virus73, Human papillomavirus52, Epstein-Barr52, BK Polyomavirus74, and Sindbis virus73.
Ivermectin inhibits importin-α/β-dependent nuclear import of viral proteins66,68,69,75, shows spike-ACE2 disruption at 1nM with microfluidic diffusional sizing33, binds to glycan sites on the SARS-CoV-2 spike protein preventing interaction with blood and epithelial cells and inhibiting hemagglutination36,76, shows dose-dependent inhibition of wildtype and omicron variants31, exhibits dose-dependent inhibition of lung injury56,61, may inhibit SARS-CoV-2 via IMPase inhibition32, may inhibit SARS-CoV-2 induced formation of fibrin clots resistant to degradation5, inhibits SARS-CoV-2 3CLpro49, may inhibit SARS-CoV-2 RdRp activity24, may minimize viral myocarditis by inhibiting NF-κB/p65-mediated inflammation in macrophages55, may be beneficial for COVID-19 ARDS by blocking GSDMD and NET formation77, shows protection against inflammation, cytokine storm, and mortality in an LPS mouse model sharing key pathological features of severe COVID-1954,78, may be beneficial in severe COVID-19 by binding IGF1 to inhibit the promotion of inflammation, fibrosis, and cell proliferation that leads to lung damage4, may minimize SARS-CoV-2 induced cardiac damage35,43, increases Bifidobacteria which play a key role in the immune system79, has immunomodulatory46 and anti-inflammatory65,80 properties, and has an extensive and very positive safety profile81.
Choudhury et al., 25 Mar 2021, peer-reviewed, 7 authors.
In Silico studies are an important part of preclinical research, however results may be very different in vivo.
This PaperIvermectinAll
Exploring the binding efficacy of ivermectin against the key proteins of SARS-CoV-2 pathogenesis: an in silico approach
Abhigyan Choudhury, Nabarun C Das, Ritwik Patra, Manojit Bhattacharya, Pratik Ghosh, Bidhan C Patra, Suprabhat Mukherjee
Aim: COVID-19 is currently the biggest threat to mankind. Recently, ivermectin (a US FDA-approved antiparasitic drug) has been explored as an anti-SARS-CoV-2 agent. Herein, we have studied the possible mechanism of action of ivermectin using in silico approaches. Materials & methods: Interaction of ivermectin against the key proteins involved in SARS-CoV-2 pathogenesis were investigated through molecular docking and molecular dynamic simulation. Results: Ivermectin was found as a blocker of viral replicase, protease and human TMPRSS2, which could be the biophysical basis behind its antiviral efficiency. The antiviral action and ADMET profile of ivermectin was on par with the currently used anticorona drugs such as hydroxychloroquine and remdesivir. Conclusion: Our study enlightens the candidature of ivermectin as an effective drug for treating COVID-19.
has relatively much higher water solubility and lipophilicity, further, having lesser skin permeation on the other hand (Supplementary Table 2 ). The three drugs included in the study are FDA-approved drugs and used for treating various parasitic (ivermectin and hydroxychloroquine) and viral (remdesivir) infections of human. However, to present the suitability of ivermectin for treating COVID-19, we have compared the pharmacological properties of ivermectin with the other two drugs. Taken together, our data on the interaction between ivermectin and viral proteins indicated that ivermectin majorly acts by interfering with the viral entry through inhibiting the function of spike protein and protease. These studies also indicate that ivermectin may also target human ACE2 and TMPRSS2 for exerting its inhibitory action over SARS-CoV-2. However, all these in silico studies require subsequent experimental validation, which could enable Ivermectin as a drug of reliance to be used for counteracting the viral growth. Conclusion Developing an effective therapeutic against COVID-19 is currently the utmost interest to the scientific communities. The present study depicts comparative binding efficacy of a promising FDA-approved drug, ivermectin, against major pathogenic proteins of SARS-CoV-2 and their human counterparts involved in host-pathogen interaction. Herein, our in silico data have indicated that ivermectin efficiently utilizes viral spike protein, main protease, replicase and..
References
Beigel, Nam, Adams, Advances in respiratory virus therapeutics -a meeting report from the 6th ISIRV Antiviral Group conference, Antiviral Res
Caly, Druce, Catton, Jans, Wagstaff, The FDA-approved drug ivermectin inhibits the replication of SARS-CoV-2 in vitro, Antiviral Res
Cao, COVID-19: immunopathology and its implications for therapy, Nat. Rev. Immunol
Chaccour, Kobylinski, Bassat, Ivermectin to reduce malaria transmission: a research agenda for a promising new tool for elimination, Malar. J
Choudhury, Das, Patra, Mukherjee, In silico analyses on the comparative sensing of SARS-CoV-2 mRNA by the intracellular TLRs of humans, J. Med. Virol
Choudhury, Mukherjee, 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
Eweas, Alhossary, As, Molecular docking reveals ivermectin and remdesivir as potential repurposed drugs against SARS-CoV-2, Front. Microbiol
Fantini, Scala, Chahinian, Yahi, Structural and molecular modelling studies reveal a new mechanism of action of chloroquine and hydroxychloroquine against SARS-CoV-2 infection, Int. J. Antimicrob. Agents
Fda, Merck, Annual Highlights Archives -Mectizan Donation Program
Formiga, Leblanc, Souza Rebouc ¸as, Farias, Oliveira et al., Ivermectin: an award-winning drug with expected antiviral activity against COVID-19, J. Control. Rel
Gautret, Lagier, Parola, Hydroxychloroquine and azithromycin as a treatment of COVID-19: results of an open-label non-randomized clinical trial, Int. J. Antimicrob. Agents
Gordon, Tchesnokov, Woolner, Remdesivir is a direct-acting antiviral that inhibits RNA-dependent RNA polymerase from severe acute respiratory syndrome coronavirus 2 with high potency, J. Biol. Chem
Heidary, Gharebaghi, Ivermectin: a systematic review from antiviral effects to COVID-19 complementary regimen, J. Antibiot. (Tokyo)
Kihara, Chen, David, Quality assessment of protein structure models, Curr. Protein Pept. Sci
Laing, Devaney, Ivermectin -old drug, new tricks?, Trends Parasitol
Lau, Khosrawipour, Kocbach, The association between international and domestic air traffic and the coronavirus (COVID-19) outbreak, J. Microbiol. Immunol. Infect
Lehrer, Rheinstein, Ivermectin docks to the SARS-CoV-2 spike receptor-binding domain attached to ACE2, vivo (Athens, Greece)
Li, Zhao, Zhan, Quantitative proteomics reveals a broad-spectrum antiviral property of ivermectin, benefiting for COVID-19 treatment, J. Cell. Physiol
López-Blanco, Aliaga, Quintana-Ortí, Chacón, iMODS: internal coordinates normal mode analysis server, Nucleic Acids Res
Mason, Pathogenesis of COVID-19 from a cell biology perspective, Eur. Respir. J
Mousavizadeh, Ghasemi, Genotype and phenotype of COVID-19: their roles in pathogenesis, J. Microbiol. Immunol. Infect
Mukherjee, Mukherjee, Gayen, Roy, Babu, Metabolic inhibitors as antiparasitic drugs: pharmacological, biochemical and molecular perspectives, Curr. Drug Metab
Nicolas, Maia, Bassat, Safety of oral ivermectin during pregnancy: a systematic review and meta-analysis, Lancet. Glob. Heal
Ong, Tan, Chia, Air, surface environmental, and personal protective equipment contamination by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) from a symptomatic patient, JAMA
Patra, Das, Mukherjee, Targeting human TLRs to combat COVID-19: a solution?, J. Med. Virol
Peng, Xu, Li, Cheng, Zhou et al., Transmission routes of 2019-nCoV and controls in dental practice, Int. J. Oral Sci
Rizzo, Ivermectin, antiviral properties and COVID-19: a possible new mechanism of action, Naunyn-Schmiedebergs Arch. Pharmacol
Rothan, Byrareddy, The epidemiology and pathogenesis of coronavirus disease (COVID-19) outbreak, J. Autoimmun
Swargiary, Ivermectin as a promising RNA-dependent RNA polymerase inhibitor and a therapeutic drug against SARS-CoV2: evidence from in silico studies, Research Square, doi:10.21203/rs.3.rs-73308/v1
Thomsen, Sanuku, Baea, Efficacy, safety, and pharmacokinetics of coadministered diethylcarbamazine, albendazole, and ivermectin for treatment of Bancroftian Filariasis, Clin. Infect. Dis
Walls, Park, Tortorici, Wall, Mcguire et al., Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein, Cell
Wan, Shang, Graham, Baric, Li, Receptor recognition by the novel coronavirus from Wuhan: an analysis based on decade-long structural studies of SARS coronavirus, J. Virol
Who, WHO Coronavirus Disease (COVID-19) Situation Reports
Yi, Lagniton, Ye, Li, Xu, COVID-19: what has been learned and to be learned about the novel coronavirus disease, Int. J. Biol. Sci
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