König M, Lengsfeld T, Pauly T, Stark R, Thiel H J
Federal Research Centre for Virus Diseases of Animals, Tübingen, Germany.
J Virol. 1995 Oct;69(10):6479-86. doi: 10.1128/JVI.69.10.6479-6486.1995.
To study which proteins of classical swine fever virus (CSFV) are able to confer protective immunity in swine, N-terminal autoprotease, viral core protein, and the three structural glycoproteins were expressed via vaccinia virus recombinants (VVR). CSFV proteins synthesized in cells infected with VVR showed migration characteristics on sodium dodecyl sulfate gels identical to those of their respective CSFV counterparts. Apparently authentic dimerization of the recombinant glycoproteins was observed. The glycoproteins E0 and E2 were detected on the surfaces of VVR-infected cells. In protection experiments, swine were immunized with the different VVR, and the generation of humoral immune response was monitored. Only animals vaccinated with VVR expressing E0 and/or E2 resisted a lethal challenge infection with CSFV. Glycoprotein E0 represents a second determinant for the induction of protective immunity against classical swine fever.
为研究经典猪瘟病毒(CSFV)的哪些蛋白能够在猪体内产生保护性免疫,通过痘苗病毒重组体(VVR)表达了N端自蛋白酶、病毒核心蛋白和三种结构糖蛋白。在感染VVR的细胞中合成的CSFV蛋白在十二烷基硫酸钠凝胶上显示出与其各自CSFV对应物相同的迁移特征。观察到重组糖蛋白明显发生了真实的二聚化。在VVR感染细胞的表面检测到了糖蛋白E0和E2。在保护实验中,用不同的VVR对猪进行免疫,并监测体液免疫反应的产生。只有接种了表达E0和/或E2的VVR的动物能够抵抗CSFV的致死性攻击感染。糖蛋白E0是诱导针对经典猪瘟的保护性免疫的第二个决定因素。