Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein.
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Schornberg K, Matsuyama S, Kabsch K, Delos S, Bouton A, White J
Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein.
J Virol. 2006 Apr;80(8):4174-8. doi: 10.1128/JVI.80.8.4174-4178.2006.
- PubMed ID
- 16571833 [ View in PubMed]
- 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.