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The potential antiviral effect of major royal jelly protein2 and its isoform X1 against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2): Insight on their sialidase activity and molecular docking
[Display omitted] •Major royal jelly protein 2 and its isoform X1 are two predicted inhibitors of SARS-CoV-2.•Major royal jelly protein 2 and its isoform X1 have sialidase activity.•Major royal jelly protein 2 and its isoform X1 might inhibit SARS-CoV-2 entry and replication.•Major royal jelly prote...
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Published in: | Journal of functional foods 2020-12, Vol.75, p.104282-104282, Article 104282 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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•Major royal jelly protein 2 and its isoform X1 are two predicted inhibitors of SARS-CoV-2.•Major royal jelly protein 2 and its isoform X1 have sialidase activity.•Major royal jelly protein 2 and its isoform X1 might inhibit SARS-CoV-2 entry and replication.•Major royal jelly protein 2 and its isoform X1 might inhibit SARS-CoV-2-induced hypoxia.
Severe acute respiratory syndrome-coronavirus (SARS-CoV)-2 is a newly emerging type of CoV. We evaluated the predicted anti-SARS-CoV-2 effect of major royal jelly protein (MRJP)2 and MRJP2 isoform X1, which recently showed high efficacy against other enveloped RNA-viruses (HCV and HIV). Some in-silico analyses have been performed to predict the impact of these proteins on viral entry, replication, and complications. These proteins have shown a high potency in sialic acid hydrolysis from the lung cells (WI-38) surface. Docking analysis showed that these proteins have a high binding affinity to viral receptor-binding sites in the receptor-binding domain, causing attachment prevention. Moreover, MRJPs can exert an inhibitory influence, via different mechanisms, for SARS-CoV-2 non-structural proteins (main and papain proteases, RNA replicase, RNA-dependent RNA polymerase, and methyltransferase). Also, they can bind to hemoglobin-binding sites on viral-nsps and prevent their hemoglobin attack. Thus, MRJP2 and MRJP2 X1 can be a promising therapy for SARS-CoV-2 infection. |
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ISSN: | 1756-4646 2214-9414 |
DOI: | 10.1016/j.jff.2020.104282 |