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

Identifieur interne : 000584 ( Main/Exploration ); précédent : 000583; suivant : 000585

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

Auteurs : Yiyan Fei ; Yung-Shin Sun [Taïwan] ; Yanhong Li ; Hai Yu ; Kam Lau ; James P. Landry ; Zeng Luo ; Nicole Baumgarth ; Xi Chen ; Xiangdong Zhu

Source :

RBID : PMC:4598760

Abstract

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.


Url:
DOI: 10.3390/biom5031480
PubMed: 26193329
PubMed Central: 4598760


Affiliations:


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Le document en format XML

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<nlm:aff id="af2-biomolecules-05-01480">Department of Physics, University of California, Davis, CA 95616, USA; E-Mails:
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<name sortKey="Chen, Xi" sort="Chen, Xi" uniqKey="Chen X" first="Xi" last="Chen">Xi Chen</name>
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<email>yhzli@ucdavis.edu</email>
(Y.L.);
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(H.Y.);
<email>edlau@ucdavis.edu</email>
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<name sortKey="Zhu, Xiangdong" sort="Zhu, Xiangdong" uniqKey="Zhu X" first="Xiangdong" last="Zhu">Xiangdong Zhu</name>
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<nlm:aff id="af2-biomolecules-05-01480">Department of Physics, University of California, Davis, CA 95616, USA; E-Mails:
<email>bacan1125@gmail.com</email>
(Y.-S.S.);
<email>jim.landry@gmail.com</email>
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<p>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.</p>
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