tetano
Editor, Senior Moderator
Angew Chem Int Ed Engl. 2016 Aug 11. doi: 10.1002/anie.201606488. [Epub ahead of print]
[h=1]Rapid Identification of the Receptor-Binding Specificity of Influenza A Viruses by Fluorogenic Glycofoldamers.[/h] He XP[SUP]1[/SUP], Zeng YL[SUP]2[/SUP], Tang XY[SUP]3[/SUP], Li N[SUP]4[/SUP], Zhou DM[SUP]5[/SUP], Chen GR[SUP]2[/SUP], Tian H[SUP]6[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The re-emergence of influenza raises a global concern that viral pandemics can unpredictably occur. However, effective approaches that can probe the infection risk of influenza viruses for humans are rare. In this work, we develop a glycofoldamer that can rapidly identify the glycan-receptor specificity of influenza viruses in a high-throughput manner. The coupling of glycan receptors that can be recognized by hemagglutinin (a surface protein on the virion capsid of influenza) to a fluorogenic-dye foldamer produces the glycofoldamers with minimal fluorescence in aqueous solution. After interaction with human-infecting virus strains for only five minutes, the fluorescence intensity of the glycofoldamer is remarkably enhanced with a blue-shifted emission peak. The probes have also proven effective for the rapid identification of 1) the human- or bird-infecting properties of influenza viruses in a high-throughput manner and 2) the receptor-specificity switch of a virus strain by mutations.
? 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
[h=4]KEYWORDS:[/h] fluorescence spectroscopy; foldamers; glycans; high-throughput screening; influenza
PMID: 27513450 DOI: 10.1002/anie.201606488
[PubMed - as supplied by publisher]
[h=1]Rapid Identification of the Receptor-Binding Specificity of Influenza A Viruses by Fluorogenic Glycofoldamers.[/h] He XP[SUP]1[/SUP], Zeng YL[SUP]2[/SUP], Tang XY[SUP]3[/SUP], Li N[SUP]4[/SUP], Zhou DM[SUP]5[/SUP], Chen GR[SUP]2[/SUP], Tian H[SUP]6[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The re-emergence of influenza raises a global concern that viral pandemics can unpredictably occur. However, effective approaches that can probe the infection risk of influenza viruses for humans are rare. In this work, we develop a glycofoldamer that can rapidly identify the glycan-receptor specificity of influenza viruses in a high-throughput manner. The coupling of glycan receptors that can be recognized by hemagglutinin (a surface protein on the virion capsid of influenza) to a fluorogenic-dye foldamer produces the glycofoldamers with minimal fluorescence in aqueous solution. After interaction with human-infecting virus strains for only five minutes, the fluorescence intensity of the glycofoldamer is remarkably enhanced with a blue-shifted emission peak. The probes have also proven effective for the rapid identification of 1) the human- or bird-infecting properties of influenza viruses in a high-throughput manner and 2) the receptor-specificity switch of a virus strain by mutations.
? 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
[h=4]KEYWORDS:[/h] fluorescence spectroscopy; foldamers; glycans; high-throughput screening; influenza
PMID: 27513450 DOI: 10.1002/anie.201606488
[PubMed - as supplied by publisher]