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Updated: Apr 26, 2026

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Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
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[Function of glycochains in virus infection]
1Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka.
Summary
Influenza A virus (IAV) replication and pandemic potential are influenced by hemagglutinin (HA) and neuraminidase (NA) functions. Glycoscience reveals how HA-sulfatide interactions and NA
Area of Science:
- Glycovirology: Investigating the role of host cell surface glycans in viral replication and pathogenesis.
- Molecular Virology: Analyzing the functions of influenza A virus (IAV) envelope glycoproteins, hemagglutinin (HA) and neuraminidase (NA).
Context:
- Influenza A virus (IAV) poses a pandemic threat through novel subtypes with altered hemagglutinin (HA) and neuraminidase (NA) antigenicities.
- IAV utilizes host cell surface sialic acids as receptors via HA binding and cleaves them using NA enzymatic activity.
Purpose:
- To elucidate the glycoscience mechanisms underlying IAV replication and pandemic potential.
- To investigate the functional roles of HA and NA in IAV pathogenesis.
Summary:
- Pandemic IAV neuraminidase (NA) exhibits low pH-stable sialidase activity, enhancing viral replication, potentially contributing to past pandemics.
- Hemagglutinin (HA) binding to host cell sulfatides, independent of sialic acid, promotes viral replication and progeny formation.
- Specific HA binding to N-glycolylneuraminic acid (Neu5Gc), present in pigs, may facilitate human IAV pandemics via genetic reassortment.
Impact:
- Identified key amino acid residues in HA responsible for Neu5Gc binding, crucial for understanding pandemic risk.
- Developed novel techniques for detecting IAV receptor specificity and infected cells, aiding in pandemic surveillance.
- Provides new insights into IAV replication and pandemic potential through a glycovirology perspective.
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