Diederich Sandra, Thiel Lena, Maisner Andrea
Institute of Virology, Philipps University of Marburg, Germany.
Virology. 2008 Jun 5;375(2):391-400. doi: 10.1016/j.virol.2008.02.019. Epub 2008 Mar 14.
The recent discovery that the Nipah virus (NiV) fusion protein (F) is activated by endosomal cathepsin L raised the question if NiV utilize pH- and protease-dependent mechanisms of entry. We show here that the NiV receptor ephrin B2, virus-like particles and infectious NiV are internalized from the cell surface. However, endocytosis, acidic pH and cathepsin-mediated cleavage are not necessary for the initiation of infection of new host cells. Our data clearly demonstrate that proteolytic activation of the NiV F protein is required before incorporation into budding virions but not after virus entry.
最近发现尼帕病毒(NiV)融合蛋白(F)可被内体组织蛋白酶L激活,这引发了一个问题,即NiV是否利用依赖pH值和蛋白酶的进入机制。我们在此表明,NiV受体埃菲林B2、病毒样颗粒和传染性NiV从细胞表面内化。然而,内吞作用、酸性pH值和组织蛋白酶介导的切割对于新宿主细胞感染的起始并非必需。我们的数据清楚地表明,NiV F蛋白在掺入出芽病毒粒子之前需要进行蛋白水解激活,但在病毒进入后则不需要。