Literature DB >> 16571833

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

Kathryn Schornberg1, Shutoku Matsuyama, Kirsten Kabsch, Sue Delos, Amy Bouton, Judith White.   

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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Year:  2006        PMID: 16571833      PMCID: PMC1440424          DOI: 10.1128/JVI.80.8.4174-4178.2006

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  22 in total

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  255 in total

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3.  Identification of a small-molecule entry inhibitor for filoviruses.

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6.  Cell adhesion-dependent membrane trafficking of a binding partner for the ebolavirus glycoprotein is a determinant of viral entry.

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7.  Ebolavirus Glycoprotein Directs Fusion through NPC1+ Endolysosomes.

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8.  Severe fever with thrombocytopenia virus glycoproteins are targeted by neutralizing antibodies and can use DC-SIGN as a receptor for pH-dependent entry into human and animal cell lines.

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