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Identification of a new carbohydrate-binding site of influenza virus

机译:鉴定流感病毒的新的碳水化合物结合位点

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It has recently been shown that the influenza virus can specifically bind the residue of a nonsialylated sulfated oligosaccharide Gal(6SO3H)β1-4GlcNAcβ (6’SLacNAc). To identify by photoaffinity labeling the virion component that binds 6’SLacNAc, we synthesized a carbohydrate probe containing a 125I 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’SLacNAcβ-OCH2CH2NHAc 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’SLacNAc-binding protein.
机译:最近显示,流感病毒可以特异性结合未唾液酸化的硫酸寡糖Gal(6SO3H)β1-4GlcNAcβ(6′SLacNAc)的残基。为了通过光亲和性标记来鉴定结合6'SLacNAc的病毒体组分,我们合成了含有125I标记的重氮基环戊二烯-2-基羰基作为糖苷配基的碳水化合物探针。根据电泳数据,标记的区域对应于较大的血凝素亚基,核衣壳蛋白和神经氨酸酶(NA)。在过量的6'SLacNAcβ-OCH2CH2NHAc糖苷存在下进行探测会导致标记强度的重新分布,并且对NA的抑制作用最大。获得的数据表明NA是病毒6'SLacNAc结合蛋白。

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