Characterization of receptor binding profiles of influenza a viruses using an ellipsometry-based label-free glycan microarray assay platform

Yiyan Fei, Yung Shin Sun, Yanhong Li, Hai Yu, Kam Lau, James P. Landry, Zeng Luo, Nicole Baumgarth, Xi Chen, Xiangdong Zhu

Research output: Contribution to journalArticle

23 Scopus citations


A key step leading to influenza viral infection is the highly specific binding of a viral spike protein, hemagglutinin (HA), with an extracellular glycan receptor of a host cell. Detailed and timely characterization of virus-receptor binding profiles may be used to evaluate and track the pandemic potential of an influenza virus strain. We demonstrate a label-free glycan microarray assay platform for acquiring influenza virus binding profiles against a wide variety of glycan receptors. By immobilizing biotinylated receptors on a streptavidin-functionalized solid surface, we measured binding curves of five influenza A virus strains with 24 glycans of diverse structures and used the apparent equilibrium dissociation constants (avidity constants, 10–100 pM) as characterizing parameters of viral receptor profiles. Furthermore by measuring binding kinetic constants of solution-phase glycans to immobilized viruses, we confirmed that the glycan-HA affinity constant is in the range of 10 mM and the reaction is enthalpy-driven.

Original languageEnglish (US)
Pages (from-to)1480-1498
Number of pages19
Issue number3
StatePublished - Jul 16 2015



  • Binding profile
  • Biosensors
  • Ellipsometry
  • Glycans
  • High-throughput
  • Influenza A virus
  • Label-free
  • Microarray
  • Reaction kinetics

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry
  • Molecular Biology

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