Zeller W, Bruns M, Lehmann-Grube F
Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie, Universität Hamburg, Federal Republic of Germany.
Virology. 1988 Jan;162(1):90-7. doi: 10.1016/0042-6822(88)90397-2.
Of a total of 17 monoclonal antibodies (MAb) directed against structural proteins of the lymphocytic choriomeningitis (LCM) virus, 3 were specific for the viral nucleoprotein (p63) and attached to the plasma membrane of infected cells, as disclosed by the indirect immunofluorescence procedure and complement-mediated cytolysis. We had previously demonstrated that a portion of the nucleoprotein (p63E) was part of the envelope of the intact virion (M. Bruns, W. Zeller, H. Rohdewohld, and F. Lehmann-Grube (1986) Virology 151, 77-85), and we now show that after external iodination of virions followed by limited proteolysis the label was attached to the smallest peptide thus obtained. If purified nucleocapsids were labeled with 125I, digested as before, and incubated with an anti-p63 MAb that has the ability to bind the surface of the infected cell, a similarly small peptide was precipitated; an antibody specific for p63 but not recognizing it on the cell surface precipitated the largest peptide and failed to bring down the small one. We conclude that the epitopes complementary to a few of our anti-p63 MAb are represented on both the virion and the surface of virus-infected cells.
在总共17种针对淋巴细胞性脉络丛脑膜炎（LCM）病毒结构蛋白的单克隆抗体（MAb）中，有3种对病毒核蛋白（p63）具有特异性，并附着于受感染细胞的质膜上，这是通过间接免疫荧光法和补体介导的细胞溶解所揭示的。我们之前已经证明，核蛋白的一部分（p63E）是完整病毒粒子包膜的一部分（M. 布伦斯、W. 泽勒、H. 罗德沃尔德和F. 莱曼 - 格鲁贝（1986年）《病毒学》151卷，77 - 85页），并且我们现在表明，在病毒粒子进行外部碘化后再进行有限的蛋白酶解，标记物附着于由此获得的最小肽段上。如果用125I标记纯化的核衣壳，像之前那样进行消化，并与能够结合受感染细胞表面的抗p63 MAb一起孵育，会沉淀出一个类似的小肽段；一种对p63具有特异性但不能在细胞表面识别它的抗体沉淀出最大的肽段，并且不能沉淀出小的肽段。我们得出结论，与我们的一些抗p63 MAb互补的表位在病毒粒子和病毒感染细胞的表面均有呈现。
