Abstract
The host adaptation of influenza virus is partly dependent on the sialic acid (SA) isoform bound by the viral hemagglutinin (HA). Avian influenza viruses preferentially bind the α-2,3 SA and human influenza viruses the α-2,6 isoform. Each isoform is predominantly associated with different surface epithelial cell types of the human upper airway. Using recombinant HAs and human tracheal airway epithelial cells in vitro and ex vivo, we show that many avian HA subtypes do not adhere to this canonical view of SA specificity. The propensity of avian viruses to adapt to human receptors may thus be more widespread than previously supposed.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Birds / virology
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Epithelial Cells / metabolism
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Epithelial Cells / virology
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Guinea Pigs
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Hemagglutinin Glycoproteins, Influenza Virus / genetics
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Hemagglutinin Glycoproteins, Influenza Virus / metabolism*
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Humans
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Influenza A virus / classification
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Influenza A virus / metabolism*
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Influenza in Birds / virology
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N-Acetylneuraminic Acid / chemistry
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N-Acetylneuraminic Acid / metabolism*
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Pandemics
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Predictive Value of Tests
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Receptors, Virus / metabolism*
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Trachea / cytology
Substances
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Hemagglutinin Glycoproteins, Influenza Virus
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Receptors, Virus
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Recombinant Proteins
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N-Acetylneuraminic Acid