Daniel C, Anderson R, Buchmeier M J, Fleming J O, Spaan W J, Wege H, Talbot P J
Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, Laval-des-Rapides, Laval, Canada.
J Virol. 1993 Mar;67(3):1185-94. doi: 10.1128/JVI.67.3.1185-1194.1993.
Numerous studies have demonstrated that the spike glycoprotein of coronaviruses bears major determinants of pathogenesis. To elucidate the antigenic structure of the protein, a panel of monoclonal antibodies was studied by competitive ELISA, and their reactivities were assayed against fragments of the murine coronavirus murine hepatitis virus strain A59 S gene expressed in prokaryotic vectors. An immunodominant linear domain was localized within the predicted stalk, S2, of the peplomer. It is recognized by several neutralizing antibodies. Other domains were also identified near the proteolytic cleavage site, in the predicted globular head, S1, and in another part of the stalk. Furthermore, competition results suggest that the immunodominant functional domain forms part of a complex three-dimensional structure. Surprisingly, some antibodies which have no antiviral biological activities were shown to bind the immunodominant neutralization domain.
众多研究表明，冠状病毒的刺突糖蛋白是发病机制的主要决定因素。为阐明该蛋白的抗原结构，通过竞争ELISA研究了一组单克隆抗体，并检测了它们对在原核载体中表达的鼠冠状病毒鼠肝炎病毒A59株S基因片段的反应性。一个免疫显性线性结构域定位于纤突蛋白预测的柄部S2内。它可被几种中和抗体识别。在蛋白水解切割位点附近、预测的球状头部S1以及柄部的另一部分也鉴定出了其他结构域。此外，竞争结果表明，免疫显性功能结构域构成复杂三维结构的一部分。令人惊讶的是，一些没有抗病毒生物学活性的抗体也被证明能结合免疫显性中和结构域。
