在昆虫细胞中合成的牛冠状病毒S刺突（纤突）糖蛋白分析。
Analysis of the S spike (peplomer) glycoprotein of bovine coronavirus synthesized in insect cells.
作者信息
Yoo D, Parker M D, Babiuk L A
机构信息
Department of Veterinary Microbiology, University of Saskatchewan, Saskatoon, Canada.
出版信息
Virology. 1990 Nov;179(1):121-8. doi: 10.1016/0042-6822(90)90281-u.
Abstract
The bovine coronavirus (BCV) spike glycoprotein precursor (S, formerly termed peplomer) and its two subunit polypeptides (S1 and S2) were individually expressed in Spodoptera frugiperda (Sf9) insect cells. Each recombinant baculovirus expressed both glycosylated (S, 170K; S1, 95K; S2, 80K) and unglycosylated (S0, 140K; S10, 75K; and S20, 65K) forms of BCV spike polypeptides in Sf9 cells. The mature 95K S1 polypeptide was secreted whereas the S and S2 polypeptides remained cell-associated. The S precursor was partially cleaved in Sf9 cells, and the resulting S1 was also released into the medium. Neutralizing monoclonal antibodies representing two antigenic domains bound to recombinant S and S1 but not the S2 polypeptides, indicating that two major epitopes for BCV neutralization are located on the S1 subunit.
摘要
牛冠状病毒（BCV）刺突糖蛋白前体（S，以前称为纤突）及其两个亚基多肽（S1和S2）分别在草地贪夜蛾（Sf9）昆虫细胞中表达。每种重组杆状病毒在Sf9细胞中均表达糖基化形式（S，170K；S1，95K；S2，80K）和非糖基化形式（S0，140K；S10，75K；S20，65K）的BCV刺突多肽。成熟的95K S1多肽被分泌，而S和S2多肽仍与细胞相关。S前体在Sf9细胞中被部分切割，产生的S1也释放到培养基中。代表两个抗原结构域的中和单克隆抗体与重组S和S1结合，但不与S2多肽结合，这表明BCV中和的两个主要表位位于S1亚基上。
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