Bruns M, Martínez Peralta L, Lehmann-Grube F
J Gen Virol. 1983 Mar;64 Pt 3:599-611. doi: 10.1099/0022-1317-64-3-599.
Analysis of radioactively labelled and highly purified infectious lymphocytic choriomeningitis (LCM) virus by polyacrylamide gel electrophoresis (PAGE) revealed 12 components which, according to their apparent molecular weight and glycosylation status, were designated as p19, p25, p26, gp35, p38, gp44, gp60, p63, p77, gp85, gp130, and p200. As shown by immunoprecipitation, they all bound to rabbit anti-LCM virus antibodies. Three proteins, namely gp35 (= 'GP-2'), gp44 (= 'GP-1') and p63 (= 'NP'), had previously been described by others as major constituents of the virion. Our results confirm this and suggest that gp60, p77, gp85, and p200 are further distinct structural proteins. In contrast, p25 and p38 appear to be cleavage or degradation products of p63; p19 and p26 seem to belong to gp60, which could be the monomeric form of a dimer, gp130. Peptide mapping by limited proteolysis revealed considerable overlapping of amino acid sequences among the major glycoproteins with one peptide being common to all. From the results of PAGE performed after external labelling of intact virions, we conclude that gp44, gp60, and gp85 (but not gp35) form the surface of the virus envelope. Analytical isoelectric focusing under non-reducing conditions has shown that the major glycoproteins appeared to consist of several components with different isoelectric points.
通过聚丙烯酰胺凝胶电泳（PAGE）对放射性标记且高度纯化的感染性淋巴细胞性脉络丛脑膜炎（LCM）病毒进行分析，结果显示有12种成分，根据其表观分子量和糖基化状态，分别命名为p19、p25、p26、gp35、p38、gp44、gp60、p63、p77、gp85、gp130和p200。免疫沉淀结果表明，它们都能与兔抗LCM病毒抗体结合。之前其他人曾将三种蛋白质，即gp35（=“GP-2”）、gp44（=“GP-1”）和p63（=“NP”）描述为病毒粒子的主要成分。我们的结果证实了这一点，并表明gp60、p77、gp85和p200是另外几种不同的结构蛋白。相比之下，p25和p38似乎是p63的裂解或降解产物；p19和p26似乎属于gp60，而gp60可能是二聚体gp130的单体形式。通过有限蛋白酶解进行的肽图谱分析显示，主要糖蛋白之间的氨基酸序列有相当程度的重叠，有一种肽段是所有糖蛋白共有的。根据对完整病毒粒子进行外部标记后进行的PAGE结果，我们得出结论，gp44、gp60和gp85（但不包括gp35）构成病毒包膜表面。在非还原条件下进行的分析性等电聚焦表明，主要糖蛋白似乎由几种具有不同等电点的成分组成。
