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内体组织蛋白酶在埃博拉病毒糖蛋白介导的病毒进入过程中的作用

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

作者信息

Schornberg Kathryn, Matsuyama Shutoku, Kabsch Kirsten, Delos Sue, Bouton Amy, White Judith

机构信息

Department of Microbiology, University of Virginia, 1300 Jefferson Park Ave., Charlottesville, Virginia 22908-0734, USA.

出版信息

J Virol. 2006 Apr;80(8):4174-8. doi: 10.1128/JVI.80.8.4174-4178.2006.

Abstract

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 siRNA, 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.

摘要

利用化学抑制剂和小干扰RNA(siRNA),我们证实了组织蛋白酶B(CatB)和组织蛋白酶L(CatL)在埃博拉病毒糖蛋白(GP)介导的感染中的作用。用CatB和CatL处理埃博拉病毒GP假病毒会使GP1从130 kDa的蛋白转变为19 kDa的蛋白。具有19 kDa GP1的病毒显示出显著增强的感染能力,并且对CatB抑制剂和siRNA的作用具有很大抗性,但它仍然需要低pH依赖性的内体/溶酶体功能。这些及其他结果支持了一个模型,即CatB和CatL通过产生一种19 kDa的中间体来引发GP,该中间体可被一种尚未确定的内体/溶酶体酶作用以触发融合。

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