Publikationsdatenbank

Glycoprotein B of equine herpesvirus type 1 (EHV-1) has two recognition sites for subtilisin-like proteases that are cleaved by furin (2016)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Spiesschaert, Bart (WE 5)

Stephanowitz, Heike

Krause, Eberhard

Osterrieder, Nikolaus (WE 5)

Azab, Walid (WE 5)

Quelle

The journal of general virology; 97(5) — S. 1218–1228

ISSN: 0022-1317

Verweise

DOI: 10.1099/jgv.0.000418

Pubmed: 26843465

Kontakt

Institut für Virologie

Robert-von-Ostertag-Str. 7-13
Gebäude 35
14163 Berlin
+49 30 838 51833
viro@zedat.fu-berlin.de

Abstract / Zusammenfassung

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 is cleaved at two positions, 518RRRR521 and 544RLHK547, and that the 28 amino acids between the two sites are 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 is 13 amino acids downstream of that previously identified.