z-logo
open-access-imgOpen Access
Blockage of Filoviral Glycoprotein Processing by Use of a Protein‐Based Inhibitor
Author(s) -
Ute Ströher,
Laura Willihnganz,
François Jean,
Heinz Feldmann
Publication year - 2007
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1086/520592
Subject(s) - furin , glycoprotein , virology , infectivity , proteases , virus , ebola virus , biology , viral replication , ns2 3 protease , cleavage (geology) , biochemistry , enzyme , paleontology , fracture (geology)
Cleavage of the glycoproteins of many virus species by furin and other host cell proteases is required for virus infectivity and, hence, determines viral pathogenicity. Proteolytic processing of Marburg virus and Ebola virus glycoproteins is also mediated by furin; however, for Ebola virus, in contrast to other viruses, glycoprotein cleavage is dispensable for replication in vitro, as has been shown in previous studies. In the present study, by use of a highly potent and selective furin inhibitor, we demonstrate that glycoprotein cleavage inhibition results in a minimal reduction in the virus titer that is insufficient to block filoviral replication. Thus, furin inhibitors are unlikely to be effective in the treatment of filoviral infections.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom