Synthesis of neuraminidase-resistant sialoside-modified three-way junction DNA and its binding ability to various influenza viruses
Copyright policy )Synthesis of neuraminidase-resistant sialoside-modified three-way junction DNA and its binding ability to various influenza viruses
Natural sialic acid-modified compounds are capable of targeting influenza virus hemagglutinin (HA). However, these compounds have limited inhibitory effect because natural O-glycoside bond in these compounds are prone to be cleaved by neuraminidase (NA) on the surface of viruses. In this study, we synthesized NA-resistant sialoside that included unnatural S-glycoside bonds and modified this sialoside on a three-way junction (3WJ) DNA to display complementary distribution to its binding sites on a HA trimer. This S-glycoside-containing sialoside-modified 3WJ DNA showed certain NA resistance and maintained high binding affinity. Importantly, our observations showed that substituting natural O-glycoside with unnatural S-glycoside did not affect the binding affinity of the sialoside-modified 3WJ DNA for viruses. Thus, this study is an important step forward in the development of NA-resistant sialoside derivatives for more effective detection and inhibition of infection by a broad spectrum of viruses.
- Osaka University Japan
- Kobe University Japan
Protein Conformation, alpha-Helical, Binding Sites, Base Sequence, Protein Stability, Neuraminidase, Hemagglutinin Glycoproteins, Influenza Virus, DNA, Solutions, Proteolysis, Sialic Acids, Nucleic Acid Conformation, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Glycosides, Protein Multimerization, Protein Binding
Protein Conformation, alpha-Helical, Binding Sites, Base Sequence, Protein Stability, Neuraminidase, Hemagglutinin Glycoproteins, Influenza Virus, DNA, Solutions, Proteolysis, Sialic Acids, Nucleic Acid Conformation, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Glycosides, Protein Multimerization, Protein Binding
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