Schornberg Kathryn, Matsuyama Shutoku, Kabsch Kirsten, Delos Sue, Bouton Amy, White Judith
Department of Microbiology, University of Virginia, 1300 Jefferson Park Ave., Charlottesville, Virginia 22908-0734, USA.
J Virol. 2006 Apr;80(8):4174-8. doi: 10.1128/JVI.80.8.4174-4178.2006.
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.
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。