Kuroki K, Floreani M, Mimms L T, Ganem D
Department of Microbiology and Immunology, University of California, San Francisco 94143.
Virology. 1990 Jun;176(2):620-4. doi: 10.1016/0042-6822(90)90032-m.
The large (L) surface glycoprotein of hepatitis B virus is an important component of the virion envelope derived from translation initiation at the 5' end of the PreS1 domain of the surface antigen open reading frame. Since key roles in virion assembly and infectivity have been postulated for this protein, further understanding of its structure and topology is important. To this end we have mapped the epitopes recognized by a panel of monoclonal antibodies specific for this polypeptide by examining their reactivity with a series of deletion mutants of the PreS1 region expressed in cultured cells. On the basis of this and other techniques, the antibodies fall into two groups mapping to two distinct epitopes spanning residues 27-35 and 72-78, respectively. Immunoprecipitation studies indicate that both regions are exposed on the surface of HBV-encoded particles.
乙型肝炎病毒的大(L)表面糖蛋白是病毒粒子包膜的重要组成部分,它由表面抗原开放阅读框的前S1结构域5'端的翻译起始产生。由于该蛋白在病毒粒子组装和感染性中被假定起着关键作用,因此进一步了解其结构和拓扑结构很重要。为此,我们通过检测一组针对该多肽的单克隆抗体与在培养细胞中表达的一系列前S1区域缺失突变体的反应性,绘制了这些抗体识别的表位图谱。基于此及其他技术,这些抗体分为两组,分别对应于跨越第27 - 35位和第72 - 78位残基的两个不同表位。免疫沉淀研究表明,这两个区域均暴露于乙肝病毒编码颗粒的表面。