Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein.

Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein.
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DOI:
10.1016/j.virol.2006.01.028
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发表时间:
2006-06-05
期刊:
影响因子:
3.7
通讯作者:
Liu DX
Liu DX
中科院分区:
医学3区
文献类型:
--
作者:
Liao Y;Yuan Q;Torres J;Tam JP;Liu DX

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一组不同的溶细胞动物病毒编码小的疏水蛋白,以改变宿主细胞膜在感染周期中对离子和小分子的通透性。在这项研究中,我们发现SARS冠状病毒E蛋白在哺乳动物细胞中的表达改变了这些细胞的膜通透性。免疫荧光染色和细胞分级研究表明,该蛋白是一种完整的膜蛋白。它主要定位于内质网和高尔基体。这种蛋白质可以转运到细胞表面,并与脂筏部分相关。进一步的生化特征表明,该蛋白是通过三个半胱氨酸残基上的棕榈酰化进行翻译后修饰的。系统诱变研究证实,SARS-CoV E蛋白的膜通透性与其跨膜区有关。
A diverse group of cytolytic animal viruses encodes small, hydrophobic proteins to modify host cell membrane permeability to ions and small molecules during their infection cycles. In this study, we show that expression of the SARS-CoV E protein in mammalian cells alters the membrane permeability of these cells. Immunofluorescent staining and cell fractionation studies demonstrate that this protein is an integral membrane protein. It is mainly localized to the ER and the Golgi apparatus. The protein can be translocated to the cell surface and is partially associated with lipid rafts. Further biochemical characterization of the protein reveals that it is posttranslationally modified by palmitoylation on all three cysteine residues. Systematic mutagenesis studies confirm that the membrane permeabilizing activity of the SARS-CoV E protein is associated with its transmembrane domain.
DOI: 10.1074/jbc.m009731200
发表时间: 2001-05-18
期刊: The Journal of biological chemistry
影响因子: --
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