Molecular Docking of Potential Inhibitors for Influenza H7N9

Abstract

As a new strain of virus emerged in 2013, avian influenza A (H7N9) virus is a threat to the public health, due to its high lethality and pathogenicity. Furthermore, H7N9 has already generated various mutations such as neuraminidase R294K mutation which could make the anti-influenza oseltamivir less effective or ineffective. In this regard, it is urgent to develop new effective anti-H7N9 drug. In this study, we used the general H7N9 neuraminidase and oseltamivir-resistant influenza virus neuraminidase as the acceptors and employed the small molecules including quercetin, chlorogenic acid, baicalein, and oleanolic acid as the donors to perform the molecular docking for exploring the binding abilities between these small molecules and neuraminidase. The results showed that quercetin, chlorogenic acid, oleanolic acid, and baicalein present oseltamivir-comparable high binding potentials with neuraminidase. Further analyses showed that R294K mutation in neuraminidase could remarkably decrease the binding energies for oseltamivir, while other small molecules showed stable binding abilities with mutated neuraminidase. Taken together, the molecular docking studies identified four potential inhibitors for neuraminidase of H7N9, which might be effective for the drug-resistant mutants.

Antiviral activity of chlorogenic acid against influenza A (H1N1/H3N2) virus and its inhibition of neuraminidase

“…Moreover, intravenous injection of CHA could be an optional administration route. Taken together, the antiviral effects of CHA against influenza virus were demonstrated in this study, which agrees with findings of previous studies1723242526. Importantly, CHA could be the potential antiviral material basis of Lonicera japonica Thunb34, Reduning35 and Shuanghuanglian injection36.…”

“…CHA was reported to reduced serum hepatitis B virus level in vivo 20. Results from molecular docking experiments indicated that CHA could be a potential NAI of influenza virus H1N123, H5N124 and H7N925. It was reported that CHA could recover cell viability and increase survival rate in H1N1-infected mice23.…”

Five Novel Non-Sialic Acid-Like Scaffolds Inhibit In Vitro H1N1 and H5N2 Neuraminidase Activity of Influenza a Virus

“…The experiments with the four neuraminidases were carried out in presence of the reference drug zanamivir. The catalytic residues within the active sites were identified as R118, R292 and R371 at subsite S1 and D151 at subsite S2, R152 at subsite S3, and E276 [ 9 , 17 , 36 , 37 ]. They are all interacting with zanamivir whose binding mode allows the drug to tightly attach to the viral enzyme and strongly inhibit the enzymatic activity, since the aforementioned residues are necessary for natural substrate recognition ( Figure 4 ).…”

Iron Chelation Properties of Green Tea Epigallocatechin‐3‐Gallate (EGCG) in Colorectal Cancer Cells: Analysis on Tfr/Fth Regulations and Molecular Docking

“…is is supported by a number of studies which predicted the high binding ability (indicated as highly negative docking scores) of small molecules to protein of interest can be correlated to their protein inhibitory property, which resulted in downregulation of protein as observed in in vitro studies and comparable with known inhibitor for that particular protein [41][42][43]. Binding of ligand (EGCG) to a protein (FtH) may result in inhibition of the protein expression, which simultaneously will downregulate the expression of the protein.…”