Literature DB >> 36175625

Lectin Staining to Detect Human and Avian Influenza Virus Receptors in the Airway of Nonhuman Primates.

Misako Nakayama1, Yasushi Itoh2.   

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.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Sialic acid; airway; immunofluorescence; influenza virus; lectin; nonhuman primates; receptor

Mesh:

Substances:

Year:  2022        PMID: 36175625     DOI: 10.1007/978-1-0716-2635-1_4

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  2 in total

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2.  Influenza virus A/Anhui/1/2013 (H7N9) replicates efficiently in the upper and lower respiratory tracts of cynomolgus macaques.

Authors:  Emmie de Wit; Angela L Rasmussen; Friederike Feldmann; Trenton Bushmaker; Cynthia Martellaro; Elaine Haddock; Atsushi Okumura; Sean C Proll; Jean Chang; Don Gardner; Michael G Katze; Vincent J Munster; Heinz Feldmann
Journal:  mBio       Date:  2014-08-12       Impact factor: 7.867

  2 in total

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