Abstract
Hemagglutinin (HA) on the surface of influenza viruses binds to sialic acids, mainly N-acetylneuraminic acid (Neu5Ac) or N-glycolylneuraminic acid. Neu5Ac and N-glycolylneuraminic acid lie at the terminal end of sugar chains on the cell surface. Human influenza viruses preferentially bind to sialic acids bound to galactose by the alpha2-6 linkage (Neu5Acα2-6Gal), abundant in the human airway. In contrast, avian influenza viruses preferentially bind to Neu5Acα2-3Gal, abundant in the intestine of ducks. Sambucus nigra lectin (SNA) and Maackia amurensis lectin (MAA) bind to Neu5Acα2-6Gal and Neu5Acα2-3Gal, respectively. These two lectins have therefore been applied to detect sialic acids on the airway epithelium of animals.
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M.N. is supported by a grant for female researchers from The Naito Foundation and Grants-in-Aid for Scientific Research (20K16217).
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Nakayama, M., Itoh, Y. (2022). Lectin Staining to Detect Human and Avian Influenza Virus Receptors in the Airway of Nonhuman Primates. In: Suzuki, Y. (eds) Glycovirology. Methods in Molecular Biology, vol 2556. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2635-1_4
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DOI: https://doi.org/10.1007/978-1-0716-2635-1_4
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