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Journal of Virology, April 2006, p. 4174-4178, Vol. 80, No. 8
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.8.4174-4178.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Role of Endosomal Cathepsins in Entry Mediated by the Ebola Virus Glycoprotein

Kathryn Schornberg,1 Shutoku Matsuyama,2 Kirsten Kabsch,2 Sue Delos,2 Amy Bouton,1*,{dagger} and Judith White1,2*

Departments of Microbiology,1 Cell Biology, University of Virginia, Charlottesville, Virginia 22908-07342

Received 17 December 2005/ Accepted 29 January 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.

* Corresponding author. Mailing address: University of Virginia, 1300 Jefferson Park Ave., Charlottesville, VA 22908-0734. Phone: (434) 924-2593. Fax: (434) 982-3912. E-mail for A. Bouton: ahb8y{at}virginia.edu; E-mail for J. White: jw7g{at}virginia.edu.

{dagger} Equal contributors.

Journal of Virology, April 2006, p. 4174-4178, Vol. 80, No. 8
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.8.4174-4178.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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