Characterization of a large, proteolytically processed cowpox virus membrane glycoprotein conserved in most chordopoxviruses.
Characterization of a large, proteolytically processed cowpox virus membrane glycoprotein conserved in most chordopoxviruses.
复制标题
大多数脊索痘病毒中保守的大型、蛋白水解加工的牛痘病毒膜糖蛋白的表征。
DOI：
10.1016/j.virol.2015.04.014
复制
发表时间：
2015
期刊：
影响因子：
3.7
通讯作者：
Moss,Bernard
中科院分区：
文献类型：
--
作者：
Reynolds,SaraE;Moss,Bernard
大多数痘病毒蛋白是高度保守的，并且对于复制中的基本步骤是必需的，或者是不太保守的，并且参与宿主相互作用。由牛痘病毒编码的CPXV 219蛋白的同源物存在于几乎所有的脊索痘病毒属中，并且一些物种具有多个拷贝。CPXV 219同源物的估计质量大于200 kDa，使其成为已知最大的痘病毒蛋白。我们发现，CPXV 219在感染早期表达，并切割成N-和C-末端片段，保持相关。该蛋白具有一个信号肽，并通过分泌途径，其中广泛的糖基化和蛋白水解裂解发生。CPXV 219通过免疫荧光显微镜定位于内质网、高尔基体和质膜。在非透化细胞中，CPXV 219可接近外部抗体和生物素化。不表达CPXV 219的突变体在细胞培养中正常复制，并在小鼠呼吸道感染模型中保留毒力。
Most poxvirus proteins are either highly conserved and essential for basic steps in replication or less conserved and involved in host interactions. Homologs of the CPXV219 protein, encoded by cowpox virus, are present in nearly all chordopoxvirus genera and some species have multiple copies. The CPXV219 homologs have estimated masses of greater than 200 kDa, making them the largest known poxvirus proteins. We showed that CPXV219 was expressed early in infection and cleaved into N- and C-terminal fragments that remained associated. The protein has a signal peptide and transited the secretory pathway where extensive glycosylation and proteolytic cleavage occurred. CPXV219 was located by immunofluorescence microscopy in association with the endoplasmic reticulum, Golgi apparatus and plasma membrane. In non-permeabilized cells, CPXV219 was accessible to external antibody and biotinylation. Mutants that did not express CPXV219 replicated normally in cell culture and retained virulence in a mouse respiratory infection model.