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...
Gespeichert in:
Veröffentlicht in: | Russian journal of bioorganic chemistry 2008-09, Vol.34 (5), p.642-646 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
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 |