Identification of a new carbohydrate-binding site of influenza virus

It has recently been shown that the influenza virus can specifically bind the residue of a nonsialylated sulfated oligosaccharide Gal(6SO 3 H)β1-4GlcNAcβ (6’ S LacNAc). To identify by photoaffinity labeling the virion component that binds 6’ S LacNAc, we synthesized a carbohydrate probe containing a...

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Veröffentlicht in:Russian journal of bioorganic chemistry 2008-09, Vol.34 (5), p.642-646
Hauptverfasser: Parfinovich, E. V., Mochalova, L. V., Molotkovsky, Yul. G., Bovin, N. V., Vodovozova, E. L.
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Sprache:eng
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Zusammenfassung:It has recently been shown that the influenza virus can specifically bind the residue of a nonsialylated sulfated oligosaccharide Gal(6SO 3 H)β1-4GlcNAcβ (6’ S LacNAc). To identify by photoaffinity labeling the virion component that binds 6’ S LacNAc, we synthesized a carbohydrate probe containing a 125 I labeled diazocyclopentadien-2-yl carbonyl group as an aglycone. According to the electrophoretic data, the labeled areas corresponded to a large hemagglutinin subunit, a nucleocapsid protein, and neuraminidase (NA). Probing in the presence of an excess of 6’ S LacNAcβ-OCH 2 CH 2 NHAc glycoside resulted in redistribution of the labeling intensity, with the maximum inhibition being observed for NA. The data obtained indicate that NA is a viral 6’ S LacNAc-binding protein.
ISSN:1068-1620
1608-330X
DOI:10.1134/S1068162008050154