Peters J E, DiCapua R A
Intervirology. 1978;9(4):231-42. doi: 10.1159/000148941.
The agglutination of chicken erythrocytes by Lymantria dispar nuclear polyhedrosis virus polyhedrin has been shown to provide specific virus identification. Selected mono- and oligosaccharides, present in blood group substances, were assayed by the Land-steiner hapten inhibition technique for specific inhibition of polyhedrin hemagglutination. N-acetylgalactosamine and N-acetylglucosamine inhibit to the greatest extent; galactosamine, glucosamine and fucose to a lesser extent. The hapten inhibition data suggest that a monosaccharide possessing an equatorial 2-acetamido group interacts most avidly with the polyhedrin-combining site. Bergold demonstrated that the polyhedrin dissociates into six subunits at a pH greater than 10.0. Diafiltration equilibrium and Scatchard analysis indicate that N-acetylgalactosamine binds most avidly to the polyhedrin (Kd = 1.7 X 10(-6)) which contains six available sites, suggesting that one hemagglutination site resides on each subunit. Since virions derived in vivo and polyhedrin are serologically cross-reactive, this protein-carbohydrate interaction may play a role in host infectivity by providing a receptor site for virus attachment to target cells.
舞毒蛾核型多角体病毒多角体蛋白对鸡红细胞的凝集作用已被证明可用于病毒的特异性鉴定。采用兰斯泰纳半抗原抑制技术，对血型物质中存在的选定单糖和寡糖进行检测，以确定其对多角体蛋白血凝作用的特异性抑制。N-乙酰半乳糖胺和N-乙酰葡糖胺的抑制作用最强；半乳糖胺、葡糖胺和岩藻糖的抑制作用较弱。半抗原抑制数据表明，具有赤道2-乙酰氨基的单糖与多角体蛋白结合位点的相互作用最为强烈。贝戈尔德证明，在pH大于10.0时，多角体蛋白会解离成六个亚基。渗滤平衡和斯卡查德分析表明，N-乙酰半乳糖胺与含有六个可用位点的多角体蛋白结合最为紧密（解离常数Kd = 1.7×10⁻⁶），这表明每个亚基上都有一个血凝位点。由于体内产生的病毒粒子和多角体蛋白具有血清学交叉反应性，这种蛋白质-碳水化合物相互作用可能通过为病毒附着于靶细胞提供受体位点，在宿主感染中发挥作用。
