Characterization of a major virion envelope glycoprotein complex of murine cytomegalovirus and its immunological cross-reactivity with human cytomegalovirus.

Characterization of a major virion envelope glycoprotein complex of murine cytomegalovirus and its immunological cross-reactivity with human cytomegalovirus.
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鼠巨细胞病毒主要病毒颗粒包膜糖蛋白复合物的表征及其与人巨细胞病毒的免疫交叉反应性。

DOI:
10.1016/0042-6822(88)90162-6
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发表时间:
1988
期刊:
影响因子:
3.7
通讯作者:
Qualtiere,LF
Qualtiere,LF
中科院分区:
医学3区
文献类型:
--
作者:
Loh,LC;Balachandran,N;Qualtiere,LF

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用两株单抗8G5.12A和2E8.12A免疫沉淀了表观分子量分别为150K(Gp50)、105K(Gp05)和52K(Gp52)的小鼠巨细胞病毒(MCMV)病毒粒子上的3种糖蛋白。然而,在补体存在的情况下,只有8G5.12A能够中和MCMV的感染性。这三种糖蛋白可通过表面碘化反应进行放射性标记,这表明它们暴露在病毒粒子的表面。Western印迹分析表明,gp150与gp105和gp52具有相同的抗原决定簇。单抗8G5.12A与gp150、gp105反应,单抗2E8.12A与gp150、gp52反应。第三个单抗3H2.12A在Western blotts中也能与gp50和gp105反应,但不能免疫沉淀这些糖蛋白。脉冲追逐实验的数据表明,所有三种病毒粒子糖蛋白都是从一个共同的128K前体合成的,这为它们的抗原相关性提供了部分解释。此外,我们还证明了gp50、gp105和gp52之间通过二硫键形成的高分子量复合体的存在。最后,单抗8G5.12A能够从人CMV感染的WI-38细胞中免疫沉淀84K和99-110K的糖蛋白,表明鼠和人CMV包膜糖蛋白之间存在保守的决定簇。
Three glycoproteins on the murine cytomegalovirus (MCMV) virion with apparent molecular weights of 150K (gpl 50), 105K (gpl05), and 52K (gp52) were immunoprecipitated by two monoclonal antibodies (MAbs) 8G5.12A and 2E8.12A. However, only 8G5.12A was able to neutralize MCMV infectivity in the presence of complement. The accessibility of these three glycoproteins to radiolabeling by surface-iodination reactions suggested that they were exposed on the surface of the virion. Western blot analysis of the three glycoproteins showed that gp150 shared antigenic determinants with gp105 and gp52. Briefly, the MAb 8G5.12A reacted with gp150 and gp105, whereas the MAb 2E8.12A reacted with gp150 and gp52. A third MAb 3H2.12A was also found to be reactive with gpl50 and gp105 in Western blots, but was unable to immunoprecipitate these glycoproteins. Data from pulse-chase experiments suggested that all three virion glycoproteins were synthesized from a common 128K precursor, providing a partial explanation of their antigenic relatedness. Furthermore, we have demonstrated the presence of high-molecular-weight complexes formed by disulfide bonding between gpl50, gp105, and gp52. Lastly, the MAb 8G5.12A was able to immunoprecipitate 84K and 99–110K glycoproteins from human CMV-infected WI-38 cells, demonstrating that conserved determinants exist between murine and human CMV envelope glycoproteins.
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