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重组杆状病毒表达具有生物活性和抗原真实性的3型副流感病毒血凝素神经氨酸酶糖蛋白

Expression of biologically active and antigenically authentic parainfluenza type 3 virus hemagglutinin-neuraminidase glycoprotein by a recombinant baculovirus.

作者信息

van Wyke Coelingh K L, Murphy B R, Collins P L, Lebacq-Verheyden A M, Battey J F

机构信息

Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.

出版信息

Virology. 1987 Oct;160(2):465-72. doi: 10.1016/0042-6822(87)90018-3.

Abstract

The hemagglutinin-neuraminidase (HN) gene of human type 3 parainfluenza virus has been inserted into a baculovirus expression vector under the control of the polyhedrin promoter. HN protein produced in insect cells by the recombinant baculovirus appeared to be glycosylated, was transported to the cell surface, and was biologically active. All of the HN epitopes previously mapped functionally to a region(s) involved in neuraminidase and/or hemagglutination activities were conformationally unaltered on the recombinant protein. The HN produced in this system also induced a protective immune response in immunized cotton rats. From these studies we conclude that the HN expressed in insect cells represents a source of authentic HN glycoprotein suitable for structural analysis and immunization.

摘要

人3型副流感病毒的血凝素神经氨酸酶(HN)基因已被插入到受多角体蛋白启动子控制的杆状病毒表达载体中。重组杆状病毒在昆虫细胞中产生的HN蛋白似乎发生了糖基化,被转运到细胞表面,并且具有生物活性。所有先前在功能上被定位到参与神经氨酸酶和/或血凝活性的区域的HN表位在重组蛋白上的构象未发生改变。在该系统中产生的HN在免疫的棉鼠中也诱导了保护性免疫反应。从这些研究中我们得出结论,在昆虫细胞中表达的HN代表了一种适合用于结构分析和免疫接种的真实HN糖蛋白来源。

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