ArticleMolecules (Basel, Switzerland)2020
Virtual Screening Identifies Chebulagic Acid as an Inhibitor of the M2(S31N) Viral Ion Channel and Influenza A Virus.
Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
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- Antiviral Effect of Isoquercitrin against Influenza A Viral Infection via Modulating Hemagglutinin and Neuraminidase.International journal of molecular sciences · 2022Article
- Hydrophobic Residues at the Intracellular Domain of the M2 Protein Play an Important Role in Budding and Membrane Integrity of Influenza Virus.Journal of virology · 2022Article
- Recent Advances in Application of Computer-Aided Drug Design in Anti-Influenza A Virus Drug Discovery.International journal of molecular sciences · 2022Review
- Editorial to Special Issue-"Structure-Activity Relationships (SAR) of Natural Products".Molecules (Basel, Switzerland) · 2021Article
- Virtual screening of natural products as potential inhibitors of SARS-CoV-2 main protease, RNA-dependent RNA polymerase (RdRp) and Spike Protein: Database design, molecular docking and molecular dynamic study.Avicenna journal of phytomedicineArticle
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 5 countries.
Funding
Abstract
The increasing prevalence of drug-resistant influenza viruses emphasizes the need for new antiviral countermeasures. The M2 protein of influenza A is a proton-gated, proton-selective ion channel, which is essential for influenza replication and an established antiviral target. However, all currently circulating influenza A virus strains are now resistant to licensed M2-targeting adamantane drugs, primarily due to the widespread prevalence of an M2 variant encoding a serine to asparagine 31 mutation (S31N). To identify new chemical leads that may target M2(S31N), we performed a virtual screen of molecules from two natural product libraries and identified chebulagic acid as a candidate M2(S31N) inhibitor and influenza antiviral. Chebulagic acid selectively restores growth of M2(S31N)-expressing yeast. Molecular modeling also suggests that chebulagic acid hydrolysis fragments preferentially interact with the highly-conserved histidine residue within the pore of M2(S31N) but not adamantane-sensitive M2(S31). In contrast, chebulagic acid inhibits in vitro influenza A replication regardless of M2 sequence, suggesting that it also acts on other influenza targets. Taken together, results implicate chebulagic acid and/or its hydrolysis fragments as new chemical leads for M2(S31N) and influenza-directed antiviral development.
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