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Article

The Natural Oligoribonucleotides Functionalized by D-Mannitol Affected Interactions of Hemagglutinin with Glycan Receptor Indicating Anti-Influenza Activity

1
Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 03680 Kyiv, Ukraine
2
“Biocell” Subsidiary Company of Biocell Laboratories Inc. (USA), Klovskiy Uzviz 17, 03680 Kyiv, Ukraine
3
NanoBioMediacal Centre, Adam Mickiewicz University, Ul. Wszechnicy Piastowskiej 3, 61-614 Poznan, Poland
4
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Ul. Pawińskiego 5a, 02-106 Warsaw, Poland
*
Authors to whom correspondence should be addressed.
Academic Editor: Agnès Girard-Egrot
Membranes 2021, 11(10), 757; https://doi.org/10.3390/membranes11100757
Received: 31 July 2021 / Revised: 27 September 2021 / Accepted: 27 September 2021 / Published: 30 September 2021
(This article belongs to the Special Issue Biomolecules in Cell Membranes: Structure and Dynamics)
Hemagglutinin (HA), the class I influenza A virus protein is responsible for the attachment of virus particles to the cell by binding to glycan receptors, subsequent virion internalization, and cell entry. Consequently, the importance of HA makes it a primary target for the development of anti-influenza drugs. The natural oligoribonucleotides (ORNs) as well as their derivatives functionalized with D-mannitol (ORNs-D-M) possess anti-influenza properties in vitro and in vivo due to interaction with HA receptor sites. This activity suppresses the viral infection in host cells. In the present work, the complexes of ORNs and ORNs-D-M with HA protein were studied by agglutination assay, fluorescence spectroscopy, as well as molecular docking simulations. Acquired experimental data exhibited a decrease in HA titer by 32 times after incubation with the ORNs-D-M for 0.5–24 h. Quenching fluorescence intensity of the HA suggests that titration by ORNs and ORNs-D-M probably leads to changes in the HA structure. Detailed structural data were obtained with the molecular docking simulations performed for ORNs and ORNs-D-M ligands containing three and six oligoribonucleotides. The results reveal that a majority of the ORNs and ORNs-D-M bind in a non-specific way to the receptor-binding domain of the HA protein. The ligand’s affinity to the hemagglutinin was estimated at the micromolar level. Presented experimental data confirmed that both natural ORNs and functionalized ORNs-D-M inhibit the interactions between HA and glycan receptors and demonstrate anti-influenza activity. View Full-Text
Keywords: hemagglutinin; oligoribonucleotides; mannitol; molecular docking hemagglutinin; oligoribonucleotides; mannitol; molecular docking
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MDPI and ACS Style

Tkachuk, Z.; Melnichuk, N.; Nikolaiev, R.O.; Szutkowski, K.; Zhukov, I. The Natural Oligoribonucleotides Functionalized by D-Mannitol Affected Interactions of Hemagglutinin with Glycan Receptor Indicating Anti-Influenza Activity. Membranes 2021, 11, 757. https://doi.org/10.3390/membranes11100757

AMA Style

Tkachuk Z, Melnichuk N, Nikolaiev RO, Szutkowski K, Zhukov I. The Natural Oligoribonucleotides Functionalized by D-Mannitol Affected Interactions of Hemagglutinin with Glycan Receptor Indicating Anti-Influenza Activity. Membranes. 2021; 11(10):757. https://doi.org/10.3390/membranes11100757

Chicago/Turabian Style

Tkachuk, Zenoviy, Nataliia Melnichuk, Roman O. Nikolaiev, Kosma Szutkowski, and Igor Zhukov. 2021. "The Natural Oligoribonucleotides Functionalized by D-Mannitol Affected Interactions of Hemagglutinin with Glycan Receptor Indicating Anti-Influenza Activity" Membranes 11, no. 10: 757. https://doi.org/10.3390/membranes11100757

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