ArticlePloS one2014
The mechanism of poly-galloyl-glucoses preventing Influenza A virus entry into host cells.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- A plant gallotannin pentagalloyl d-glucose elicits antiviral activity against influenza A and B viruses through multi-targeting mechanisms.Archives of virology · 2026Article
- A Focus on Natural Autophagy Modulators as Potential Host-Directed Weapons Against Emerging and Re-Emerging Viruses.Medicinal research reviews · 2025Review
- Sumac Polyphenols as Pan-Herpesvirus Inhibitors.International journal of molecular sciences · 2025Article
- Antiviral effects of herbal extracts against avian influenza and Newcastle disease viruses.Open veterinary journal · 2025Review
- Novel Fermentation Strategies of Strawberry TreeInternational journal of molecular sciences · 2024Article
- Examining the interactions of Galahad™ compound with viruses to develop a novel inactivated influenza A virus vaccine.Heliyon · 2022Article
- Epigallocatechin-3-Gallate (EGCG) Inhibits SARS-CoV-2 Infection in Primate Epithelial Cells: (A Short Communication).Microbiology & infectious diseases (Wilmington, Del.) · 2021Article
- Structure Activity Related, Mechanistic, and Modeling Studies of Gallotannins containing a Glucitol-Core andRSC advances · 2015Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hemagglutinin (HA) is essential for Influenza A virus infection, but its diversity of subtypes presents an obstacle to developing broad-spectrum HA inhibitors. In this study, we investigated the molecular mechanisms by which poly-galloyl glucose (pGG) analogs inhibit influenza hemagglutinin (HA) in vitro and in silico. We found that (1) star-shaped pGG analogs exhibit HA-inhibition activity by interacting with the conserved structural elements of the receptor binding domain (RBD); (2) HA inhibition depends on the number of galloyl substituents in a pGG analog; the best number is four; and when PGG binds with two HA trimers at their conserved receptor binding domains (loop 130, loop 220, and 190-α-helix), PGG acts as a molecular glue by aggregating viral particles so as to prevent viral entry into host cells (this was revealed via an in silico simulation on the binding of penta-galloyl-glucose (PGG) with HA). pGGs are also effective on a broad-spectrum influenza A subtypes (including H1, H3, H5, H7); this suggests that pGG analogs can be applied to most influenza A subtypes as a prophylactic against influenza viral infections.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.