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• W2274001519 endingPage "172" @default.
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• W2274001519 abstract "Most therapeutical nucleic acid aptamers tend to inhibit protein-protein interactions and thereby function as antagonists. Attachment of the influenza virus surface glycoprotein hemagglutinin (HA) to sialic acid-containing host cell receptors (glycan) facilitates the initial stage of viral infection. Inhibition of the attachment may result in an antiviral effect on the proliferation of the influenza virus. To develop therapeutically interesting agents, we selected two single-stranded DNA (ssDNA) aptamers specific to the HA protein of H1N1 influenza virus (A/Puerto Rico/8/1934) through a procedure of systematic evolution of ligands by exponential enrichment. As it showed a higher binding affinity for HA protein (Kd = 78 ± 1 nM), aptamer 1 was tested for its ability to interfere with HA-glycan interactions using chicken red blood cell hemagglutination and microneutralization assays, which demonstrated that it significantly suppressed the viral infection in host cells. These results indicate that the isolated ssDNA aptamer may be developed as an antiviral agent against influenza through appropriate therapeutic formulation." @default.
• W2274001519 created "2016-06-24" @default.
• W2274001519 creator A5009530693 @default.
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• W2274001519 date "2016-06-01" @default.
• W2274001519 modified "2023-10-18" @default.
• W2274001519 title "A DNA Aptamer Against Influenza A Virus: An Effective Inhibitor to the Hemagglutinin–Glycan Interactions" @default.
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• W2274001519 doi "https://doi.org/10.1089/nat.2015.0564" @default.
• W2274001519 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26904922" @default.
• W2274001519 hasPublicationYear "2016" @default.
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