4.8 Article

Rapid Identification of the Receptor-Binding Specificity of InfluenzaA Viruses by Fluorogenic Glycofoldamers

Journal

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 55, Issue 45, Pages 13995-13999

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201606488

Keywords

fluorescence spectroscopy; foldamers; glycans; high-throughput screening; influenza

Funding

  1. 973 project [2013CB733700]
  2. National Natural Science Foundation of China [21572058, 21576088, 31200617]
  3. Knowledge Innovation Program [Y014P31503]
  4. 100 Talent Program from the Chinese Academy of Sciences [Y316P11503]
  5. Shanghai Rising-Star Program [16QA1401400]

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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.

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