title: Glycoprotein B of equine herpesvirus type 1 has two recognition sites for subtilisin-like proteases that are cleaved by furin.
abstract: Glycoprotein B (gB) of equine herpesvirus type 1 (EHV-1) is predicted to be cleaved by furin in a fashion similar to that of related herpesviruses. To investigate the contribution of furin-mediated gB cleavage to EHV-1 growth, canonical furin cleavage sites were mutated. Western blot analysis of mutated EHV-1 gB showed that it was cleaved at two positions, 518RRRR521 and 544RLHK547, and that the 28 aa between the two sites were removed after cleavage. Treating infected cells with either convertase or furin inhibitors reduced gB cleavage efficiency. Further, removal of the first furin recognition motif did not affect in vitro growth of EHV-1, while mutation of the second motif greatly affected virus growth. In addition, a second possible signal peptide cleavage site was identified for EHV-1 gB between residues 98 and 99, which was 13 aa downstream of that previously identified.
authors: Institut für Virologie, Robert von Ostertag-Haus, Zentrum für Infektionsmedizin,Freie Universität Berlin, Robert-von-Ostertag-Str. 7-13, 14163 Berlin,Germany.
authors: Bart
authors: B
authors: Spiesschaert
authors: Leibniz-Institut für Molekulare Pharmakologie,Robert-Rössle-Strasse 10, D-13125 Berlin,Germany.
authors: Heike
authors: H
authors: Stephanowitz
authors: Leibniz-Institut für Molekulare Pharmakologie,Robert-Rössle-Strasse 10, D-13125 Berlin,Germany.
authors: Eberhard
authors: E
authors: Krause
authors: Institut für Virologie, Robert von Ostertag-Haus, Zentrum für Infektionsmedizin,Freie Universität Berlin, Robert-von-Ostertag-Str. 7-13, 14163 Berlin,Germany.
authors: Nikolaus
authors: N
authors: Osterrieder
authors: Department of Virology, Faculty of Veterinary Medicine,Zagazig University,Egypt.|Institut für Virologie, Robert von Ostertag-Haus, Zentrum für Infektionsmedizin,Freie Universität Berlin, Robert-von-Ostertag-Str. 7-13, 14163 Berlin,Germany.
authors: Walid
authors: W
authors: Azab
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D045683:Furin / Q000378:metabolism*; D004861:Herpesvirus 1, Equid; D007963:Leukocytes, Mononuclear / Q000821:virology; D009154:Mutation; D011485:Protein Binding; D013381:Subtilisins / Q000737:chemistry / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D014759:Viral Envelope Proteins; C040495:glycoprotein B, Simplexvirus; D013381:Subtilisins; D045683:Furin