Bruns M, Zeller W, Rohdewohld H, Lehmann-Grube F
Virology. 1986 May;151(1):77-85. doi: 10.1016/0042-6822(86)90105-4.
Nucleocapsids (NC) of lymphocytic choriomeningitis (LCM) virus were obtained by treatment of purified infectious virus with detergent and salt at high concentrations, followed by gradient centrifugation. NC thus prepared contained 31 S RNA, 23 S RNA, and a protein with an apparent mol wt 63,000 and an isoelectric point pH 5.7 (p63), assumed to be the nucleoprotein. We had previously observed that the intact LCM virus contained two kinds of protein with mol wt 63,000 separable by their isoelectric points which were pH 5.7 and 7.7, respectively. We now found that the latter component was removed from the NC together with the glycoproteins, and labeling studies revealed that it was closely associated with the viral envelope. We have named the protein with a mol wt of 63,000 and an isoelectric point pH 7.7 p63E (E for envelope). By limited proteolysis both viral components of mol wt 63,000 could not be distinguished, indicating that they are basically identical. It appears that p63E is the phosphorylated form of p63.
通过用高浓度去污剂和盐处理纯化的感染性淋巴细胞性脉络丛脑膜炎(LCM)病毒,随后进行梯度离心,获得了该病毒的核衣壳(NC)。如此制备的NC含有31S RNA、23S RNA以及一种表观分子量为63,000且等电点为pH 5.7(p63)的蛋白质,假定其为核蛋白。我们之前观察到完整的LCM病毒含有两种分子量为63,000的蛋白质,可通过其等电点分别为pH 5.7和7.7加以区分。我们现在发现后一种成分与糖蛋白一起从NC中被去除,并且标记研究表明它与病毒包膜紧密相关。我们将分子量为63,000且等电点为pH 7.7的蛋白质命名为p63E(E代表包膜)。通过有限的蛋白酶解,无法区分两种分子量为63,000的病毒成分,这表明它们基本相同。看来p63E是p63的磷酸化形式。