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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
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Arbidol targeting influenza virus A Hemagglutinin; A comparative study

Alhassan Ali Ahmed1, Mohamed Abouzid2

  • 1University of Warsaw, Center of New Technologies (CeNT), Warsaw, Poland; Department of Bioinformatics and Computational Biology, Poznan University of Medical Sciences, Poznan, Poland.

Biophysical Chemistry
|August 13, 2021
PubMed

Influenza (flu) is a serious global health threat. The Hemagglutinin (HA) protein binds the flu virus to the sialic acids at the surface of the host cells' membrane which allows the endocytosis of the virus. Therefore, potential inhibitors can attach to the active site of HA and block the virus life-cycle. In this study, the antiviral drug arbidol (ARB) and 16 HA-subtypes were docked and analyzed to represent different approaches in predicting the conformation of protein-ligand, protein-protein, and protein-glycan complex and its binding energy. Our findings show that ARB interacts with all HA subtypes, and H7 possesses the best affinity. The next influenza pandemic could be caused by H4, H5, H6, and H14 subtypes, which prompts further studies in investigating the interaction between these particular HA subtypes and other antiviral drugs to obtain higher efficacy.

Keywords:
3D modulationArbidolHemagglutininHemagglutinin inhibitorInfluenza AMolecular docking

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