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麻疹病毒感染细胞质膜上主要组织相容性复合体及病毒抗原的定位

Mapping of the major histocompatibility complex and viral antigens on the plasma membrane of a measles virus-infected cell.

作者信息

Oldstone M B, Fujinami R S, Tishon A, Finney D, Powell H C, Lampert P W

出版信息

Virology. 1983 Jun;127(2):426-37. doi: 10.1016/0042-6822(83)90155-1.

Abstract

The two measles virus glycoproteins, the hemagglutinin and fusion protein, are expressed on the surfaces of infected cells. Although the two molecules are chemically distinct, they associate on the cell surface, judging from their ability to comigrate (co-cap). However, neither is directly complexed with the major histocompatibility (MHC) gene products, HLA-A, -B, -C or -D, on the plasma membrane, based on results from three distinct assays. First, in tests of capping, these viral glycoproteins failed to comigrate with any HLA determinant. Second, electron microscopy showed that the viral glycoproteins occupied domains on the plasma membrane distinct from MHC gene products; 125I labeling of cell surface determinants and subsequent analysis by immune precipitation and PAGE confirmed this result. Third, incubation of measles virus-infected cells in the presence of monoclonal or polyclonal antibodies to measles virus glycoproteins removed the viral glycoproteins from the cells' surfaces but did not cause a corresponding decrease in amounts of HLA molecules. These results indicate that the hemagglutinin and fusion polypeptides of measles virus lie in close association on the plasma membrane; however, neither is linked with MHC gene products.

摘要

两种麻疹病毒糖蛋白,即血凝素和融合蛋白,在受感染细胞表面表达。尽管这两种分子在化学性质上不同,但从它们共迁移(共帽化)的能力判断,它们在细胞表面相互关联。然而,根据三种不同检测的结果,在质膜上,它们都不与主要组织相容性(MHC)基因产物HLA - A、- B、- C或 - D直接复合。首先,在帽化检测中,这些病毒糖蛋白未能与任何HLA决定簇共迁移。其次,电子显微镜显示病毒糖蛋白占据质膜上与MHC基因产物不同的区域;细胞表面决定簇的125I标记以及随后通过免疫沉淀和聚丙烯酰胺凝胶电泳进行的分析证实了这一结果。第三,在存在针对麻疹病毒糖蛋白的单克隆或多克隆抗体的情况下,对感染麻疹病毒的细胞进行孵育,可从细胞表面去除病毒糖蛋白,但不会导致HLA分子数量相应减少。这些结果表明,麻疹病毒的血凝素和融合多肽在质膜上紧密关联;然而,它们都不与MHC基因产物相连。

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