Proteolysis of the Ebola Virus Glycoproteins Enhances Virus Binding and Infectivity

• DOI: 10.1128/jvi.01170-07
• Publication Date: 2007-10-11T00:39:28Z
• Authors: Rachel L. Kaletsky; Graham Simmons; Paul Bates
• Keywords: Filoviridae; Cathepsin L; VP40; Infectivity; Ebolavirus; Mononegavirales

Cellular cathepsins are required for Ebola virus infection and believed to proteolytically process the glycoprotein (GP) during entry. However, significance of cathepsin cleavage remains unclear. Here we demonstrate a role L (CatL) GP in generation stable 18-kDa GP1 viral intermediate that exhibits increased binding infectivity susceptible cell targets. Cell lymphocyte line was when CatL-proteolysed pseudovirions were used, but lymphocytes remained resistant GP-mediated infection. Genetic removal highly glycosylated mucin domain resulted similar observed with CatL-treated full-length GP, no overall enhancement or mucin-deleted virions treated CatL. These results suggest facilitates an interaction cellular receptor(s) may facilitate receptor binding. The influence CatL should be useful future studies characterizing mechanism