鼠冠状病毒纤突糖蛋白S1多肽上主要中和表位的定位
Localization of major neutralizing epitopes on the S1 polypeptide of the murine coronavirus peplomer glycoprotein.
作者信息
Takase-Yoden S, Kikuchi T, Siddell S G, Taguchi F
机构信息
National Institute of Neuroscience, NCNP, Tokyo, Japan.
出版信息
Virus Res. 1991 Mar;18(2-3):99-107. doi: 10.1016/0168-1702(91)90011-j.
Abstract
A recombinant baculovirus system has been used to express the amino terminal half of the murine coronavirus (JHMV) peplomer glycoprotein in insect cells. The expressed polypeptide is glycosylated and is recognized by a set of monoclonal antibodies (mAbs) specific for JHMV S protein. Three of these mAbs have a very high neutralizing activity for JHMV but not for other MHV strains. These results indicate that JHMV-specific, major neutralizing epitopes reside in the amino terminal S1 subunit of the peplomer glycoprotein.
摘要
一种重组杆状病毒系统已被用于在昆虫细胞中表达鼠冠状病毒（JHMV）纤突糖蛋白的氨基末端部分。所表达的多肽是糖基化的，并被一组针对JHMV S蛋白的单克隆抗体（mAb）识别。其中三种mAb对JHMV具有非常高的中和活性，但对其他MHV毒株则没有。这些结果表明，JHMV特异性的主要中和表位位于纤突糖蛋白的氨基末端S1亚基中。
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