The interaction of a series of hybridoma IgGs with reovirus particles. Demonstration that the core protein lambda 2 is exposed on the particle surface.
The interaction of a series of hybridoma IgGs with reovirus particles. Demonstration that the core protein lambda 2 is exposed on the particle surface.
复制标题
一系列杂交瘤 IgG 与呼肠孤病毒颗粒的相互作用。
DOI：
10.1016/0042-6822(81)90534-1
复制
发表时间：
1981
期刊：
影响因子：
3.7
通讯作者：
Joklik,WK
中科院分区：
文献类型：
--
作者：
Hayes,EC;Lee,PW;Miller,SE;Joklik,WK
我们最近已经描述了19个杂交瘤细胞系的分离，分泌抗呼肠孤病毒编码蛋白的IgG，其特征在于它们的特异性，判断它们的能力，从感染细胞的裂解液沉淀病毒编码的蛋白。在本文中，我们描述了这些杂交瘤分泌的IgG的特性，其与呼肠孤病毒颗粒的反应能力。针对三种呼肠孤病毒蛋白的IgG能够中和感染性、抑制血凝并沉淀/聚集呼肠孤病毒颗粒：针对多肽σ1和σ3（呼肠孤病毒衣壳外壳的两种组分）的IgG和针对多肽λ2（呼肠孤病毒核心的组分）的IgG。此外，针对多肽μ1/μ1C和μNS的IgG中的一些但不是全部也沉淀/聚集呼肠孤病毒颗粒。针对λ2的IgG具有强的中和、血凝抑制和病毒沉淀活性的事实表明，存在于呼肠孤病毒核心上并且主要或完全由λ2组成的突起或刺突穿过外壳体壳突出到呼肠孤病毒颗粒的表面。这一结论通过以下证明得到证实：在只有呼肠孤病毒外壳的已知组分被标记的条件下，多肽λ2可以通过乳过氧化物酶催化的放射性碘标记技术进行标记。
We have recently described the isolation of 19 hybridoma cell lines that secrete IgGs directed against reovirus-coded proteins, and characterized their specificities as judged by their ability to precipitate virus-coded proteins from lysates of infected cells. We describe in this paper the characterization of these hybridoma-secreted IgGs by their ability to react with reovirus particles. IgGs directed against three reovirus proteins were able to neutralize infectivity, inhibit hemagglutination, and precipitate/aggregate reovirus particles: those directed against polypeptides σ1 and σ3, both components of the outer reovirus capsid shell, and those directed against polypeptide λ2, a component of reovirus cores. In addition, some, but not all, of the IgGs directed against polypeptides μ1/μ1C and μNS also precipitate/aggregate reovirus particles. The fact that IgGs directed against λ2 possess strong neutralizing, hemagglutination inhibiting, and virus precipitating activities suggests that the projections or spikes that are present on reovirus cores and that are composed primarily or exclusively of λ2 project through the outer capsid shell to the surface of reovirus particles. This conclusion was confirmed by the demonstration that polypeptide λ2 could be labeled by means of the lactoperoxidase-catalyzed radioiodination technique under conditions when only known components of the reovirus outer capsid shell became labeled.