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Ectodomain shedding of the glycoprotein GP of Ebola virus.

Research paper by Olga O Dolnik, Valentina V Volchkova, Wolfgang W Garten, Caroline C Carbonnelle, Stephan S Becker, Jörg J Kahnt, Ute U Ströher, Hans-Dieter HD Klenk, Viktor V Volchkov

Indexed on: 23 Apr '04Published on: 23 Apr '04Published in: The EMBO Journal



Abstract

In this study, release of abundant amounts of the Ebola virus (EBOV) surface glycoprotein GP in a soluble form from virus-infected cells was investigated. We demonstrate that the mechanism responsible for the release of GP is ectodomain shedding mediated by cellular sheddases. Proteolytic cleavage taking place at amino-acid position D637 removes the transmembrane anchor and liberates complexes consisting of GP1 and truncated GP2 (GP(2delta)) subunits from the cell surface. We show that tumor necrosis factor alpha-converting enzyme (TACE), a member of the ADAM family of zinc-dependent metalloproteases, is involved in EBOV GP shedding. This finding shows for the first time that virus-encoded surface glycoproteins are substrates for ADAMs. Furthermore, we provide evidence that shed GP is present in significant amounts in the blood of virus-infected animals and that it may play an important role in the pathogenesis of infection by efficiently blocking the activity of virus-neutralizing antibodies.

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