REVERSIBLE CONFORMATIONAL-CHANGES AND FUSION ACTIVITY OF RABIES VIRUS GLYCOPROTEIN
REVERSIBLE CONFORMATIONAL-CHANGES AND FUSION ACTIVITY OF RABIES VIRUS GLYCOPROTEIN
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DOI：
10.1128/jvi.65.9.4853-4859.1991
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发表时间：
1991-09-01
影响因子：
5.4
通讯作者：
FLAMAND, A
中科院分区：
文献类型：
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作者：
GAUDIN, Y;TUFFEREAU, C;FLAMAND, A
为了了解狂犬病病毒糖蛋白（G）在病毒周期的第一步中的意义，我们研究了病毒诱导的融合和血凝的pH依赖性，以及pH酸化后病毒糖蛋白的结构和性质的改变。 我们的研究结果表明，G蛋白采用至少三种不同的配置，每一个与不同的属性。 在中性pH值，G不融合膜或血细胞凝集红细胞。 它对菠萝蛋白酶和胰蛋白酶消化不敏感。 在pH 6.4时，糖蛋白对蛋白酶变得敏感。 血凝作用达到最大值，然后随pH值急剧下降。未检测到融合。 还观察到病毒聚集。 第三种构型，在低于pH 6.1时，与融合的外观相关。 一些中和性单克隆抗体能够区分这三种构型。 在低于pH 6的条件下预孵育病毒会抑制融合，但这种抑制作用与糖蛋白的结构修饰一样，在中性pH条件下重新孵育G时是可逆的。
In an attempt to understand the implication of the rabies virus glycoprotein (G) in the first steps of the viral cycle, we studied the pH dependence of virus-induced fusion and hemagglutination, as well as modifications of the structure and properties of the viral glycoprotein following pH acidification. Our results suggest that the G protein adopts at least three distinct configurations, each associated with different properties. At neutral pH, G did not fuse membranes or hemagglutinate erythrocytes. It was insensitive to digestion with bromelain and trypsin. At pH 6.4, the glycoprotein became sensitive to proteases. Hemagglutination was at its maximum and then sharply decreased with the pH. No fusion was detected. Aggregation of virus was also observed. The third configuration, at below pH 6.1, was associated with the appearance of fusion. Some neutralizing monoclonal antibodies were able to differentiate these three configurations. Preincubation of the virus at below pH 6 inhibited fusion, but this inhibition, like the structural modifications of the glycoprotein, was reversible when G was reincubated at neutral pH.