Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein

被引：352

作者：

Schornberg, K

Matsuyama, S

Kabsch, K

Delos, S

Bouton, A

White, J

机构：

[1] Univ Virginia, Dept Microbiol, Charlottesville, VA 22908 USA

[2] Univ Virginia, Dept Cell Biol, Charlottesville, VA 22908 USA

来源：

JOURNAL OF VIROLOGY | 2006年 / 80卷 / 08期

关键词：

D O I：

10.1128/JVI.80.8.4174-4178.2006

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Using chemical inhibitors and small interfering RNA (siRNA), we have confirmed roles for cathepsin B (CatB) and cathepsin L (CatL) in Ebola virus glycoprotein (GP)-mediated infection. Treatment of Ebola virus GP pseudovirions with CatB and CatL converts GP1 from a 130-kDa to a 19-kDa species. Virus with 19-kDa GP1 displays significantly enhanced infection and is largely resistant to the effects of the CatB inhibitor and ARNA, but it still requires a low-pH-dependent endosomal/lysosomal function. These and other results support a model in which CatB and CatL prime GP by generating a 19-kDa intermediate that can be acted upon by an as yet unidentified endosomal/lysosomal enzyme to trigger fusion.

引用

收藏

页码：4174 / 4178

页数：5

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