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

      Journal of Biology

      Animals, Cathepsin B, physiology, Cathepsin L, Cathepsins, Cercopithecus aethiops, Cricetinae, Cysteine Endopeptidases, Ebolavirus, Endosomes, enzymology, RNA, Small Interfering, pharmacology, Vero Cells, Vesicular stomatitis Indiana virus, genetics, Viral Fusion Proteins

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          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.

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          Author and article information

          Journal
          16571833
          1440424
          10.1128/JVI.80.8.4174-4178.2006

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