Unusual lectin-binding properties of a herpes simplex virus type 1-specific glycoprotein
Unusual lectin-binding properties of a herpes simplex virus type 1-specific glycoprotein
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1 型单纯疱疹病毒特异性糖蛋白异常的凝集素结合特性
DOI：
10.1128/jvi.38.2.564-570.1981
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发表时间：
1981
影响因子：
5.4
通讯作者：
E. Lycke
中科院分区：
文献类型：
--
作者：
S. Olofsson;S. Jeansson;E. Lycke
从单纯疱疹病毒1型感染的细胞裂解物进行亲和层析对大豆和苹果凝集素。一种病毒特异性糖蛋白，可能是单纯疱疹病毒1型特异性gC糖蛋白，与凝集素结合，并用N-乙酰半乳糖胺洗脱。亲和层析允许高度纯化的类型特异性糖蛋白相对于宿主细胞成分和其他病毒糖蛋白。该糖蛋白的凝集素亲和模式表明寡糖中存在末端α-N-乙酰半乳糖胺，这是以前未报道的包膜病毒糖蛋白的发现。
Lysates from herpes simplex virus type 1-infected cells were subjected to affinity chromatography on soybean and Helix pomatia lectins. One of the virus-specified glycoproteins, probably the herpes simplex virus type 1-specific gC glycoprotein, bound to the lectins and was eluted with N-acetylgalactosamine. The affinity chromatography permitted a high degree of purification of the type-specific glycoprotein with respect to both host cell components and other viral glycoproteins. The lectin affinity pattern of this glycoprotein indicates the presence of a terminal alpha-N-acetylgalactosamine in an oligosaccharide, a finding not reported previously for glycoproteins of enveloped viruses.