The transmembrane domain of the infectious bronchitis virus E protein is required for efficient virus release.
The transmembrane domain of the infectious bronchitis virus E protein is required for efficient virus release.
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传染性支气管炎病毒 E 蛋白的跨膜结构域是病毒有效释放所必需的。
DOI：
10.1007/978-0-387-33012-9_33
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发表时间：
2006
影响因子：
--
通讯作者：
Youn,Soonjeon
中科院分区：
文献类型：
--
作者：
Machamer,CarolynE;Youn,Soonjeon
传染性支气管炎病毒（IBV） E蛋白是一种小蛋白，跨越一次膜，其c端在细胞质中。我们之前发现，IBV E蛋白的细胞质尾部介导其靶向高尔基膜，6以及与IBV M蛋白的相互作用。IBV E细胞质结构域的突变降低了高尔基体潴留，阻断了EM的关联和VLPs的产生。相比之下，用异源跨膜结构域完全取代IBV E蛋白的跨膜结构域对E的高尔基靶向、M与E的结合或VLPs的产生没有影响。6,7我们得出结论，蛋白质跨膜结构域的序列对其功能不重要。一些包膜病毒，包括流感病毒和人类免疫缺陷病毒，编码小的膜蛋白，在感染细胞中形成离子通道。最近有研究表明，严重急性呼吸综合征（SARS）冠状病毒的E蛋白在合成膜中形成一个阳离子特异性离子通道。这一观察结果表明，我们重新评估了IBV E突变体的跨膜结构域取代。由于离子运动的孔是由离子通道的跨膜部分形成的，因此替换该序列将会阻碍通道功能。在IBV感染克隆中将野生型E蛋白序列替换为跨膜替代的E蛋白序列后，我们恢复并鉴定了IBV感染克隆的E蛋白
The infectious bronchitis virus (IBV) E protein is a small protein that spans the membrane once, with its C-terminus in the cytoplasm. 5 We previously showed that the cytoplasmic tail of the IBV E protein mediated its targeting to Golgi membranes, 6 as well as its interaction with the IBV M protein. 7 Mutations in the cytoplasmic domain of IBV E reduced Golgi retention and blocked EM association and production of VLPs. By contrast, complete replacement of the transmembrane domain of the IBV E protein with a heterologous membrane-spanning domain had no effect on the Golgi targeting of E, the association of M with E, or the production of VLPs. 6, 7 We concluded that the sequence of the transmembrane domain of the protein was unimportant for its function. Some enveloped viruses including influenza and human immunodeficiency virus encode small membrane proteins that form ion channels in infected cells. 8 The E protein of the severe acute respiratory syndrome (SARS) coronavirus has recently been shown to form a cation-specific ion channel in synthetic membranes. 9 This observation suggested that we reevaluate the IBV E mutant with a substituted transmembrane domain. Because the pore for ion movement forms from the transmembrane segments of ion channels, replacing the sequence would be expected to block channel function. After replacing the wild-type E protein sequence for that of the transmembranesubstituted E protein in an infectious clone for IBV, we recovered and characterized the