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Literature detail

Characterization of Receptor Binding Profiles of Influenza A Viruses Using An Ellipsometry-Based Label-Free Glycan Microarray Assay Platform.

Yiyan Fei1,2 Yung-Shin Sun3,4 Yanhong Li5 Hai Yu6 Kam Lau7 James P Landry8 Zeng Luo9 Nicole Baumgarth10 Xi Chen11 Xiangdong Zhu12
Affiliations 12 institutions
  1. Key Laboratory of Micro and Nano Photonic Structures (Ministry of Education), Department of Optical Science and Engineering, Shanghai Engineering Research Center of Ultra-Precision Optical Manufacturing, Fudan University, 220 Handan Road, Shanghai 200433, China. [email protected].
  2. Department of Physics, University of California, Davis, CA 95616, USA. [email protected].
  3. Department of Physics, University of California, Davis, CA 95616, USA. [email protected].
  4. Department of Physics, Fu-Jen Catholic University, New Taipei City 24205, Taiwan. [email protected].
  5. Department of Chemistry, University of California, Davis, CA 95616, USA. [email protected].
  6. Department of Chemistry, University of California, Davis, CA 95616, USA. [email protected].
  7. Department of Chemistry, University of California, Davis, CA 95616, USA. [email protected].
  8. Department of Physics, University of California, Davis, CA 95616, USA. [email protected].
  9. Center for Comparative Medicine, University of California, Davis, CA 95616, USA. [email protected].
  10. Center for Comparative Medicine, University of California, Davis, CA 95616, USA. [email protected].
  11. Department of Chemistry, University of California, Davis, CA 95616, USA. [email protected].
  12. Department of Physics, University of California, Davis, CA 95616, USA. [email protected].
PMID 26193329 2015 Biomolecules eng epublish
PubMed DOI Browse context

Article

Publication summary

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.

binding profile biosensors ellipsometry glycans high-throughput influenza A virus label-free microarray reaction kinetics Optical Devices Animals Humans Influenza A virus Influenza A Virus, H1N1 Subtype Influenza A Virus, H5N1 Subtype Kinetics Ligands Microarray Analysis

Structured evidence records

Evidence records

1 total
Receptor Usage 1 records
Receptor Usage Extraction confidence 0.98
Key finding

Influenza A virus hemagglutinin binds to multiple glycan receptors with specific affinity constants determined using a label-free microarray assay.

Virus
IAV
Host
Not specified
Location
Not specified
Supporting text

We measured binding curves of five influenza A virus strains with 24 glycans of diverse structures and used the apparent equilibrium dissociation constants as characterizing parameters of viral receptor profiles.

Method
glycan microarray assay; ellipsometry; binding assay
Receptors
glycan receptor