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J Virol, May 1998, p. 4528-4533, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Processing of the Borna Disease Virus Glycoprotein gp94 by the Subtilisin-Like Endoprotease Furin

Jürgen A. Richt,1,* Thomas Fürbringer,1 Andreas Koch,2 Isolde Pfeuffer,1 Christiane Herden,1 Ingrid Bause-Niedrig,1 and Wolfgang Garten2

Institut für Virologie, D-35392 Giessen,1 and Institut für Virologie, D-35037 Marburg,2 Germany

Received 17 October 1997/Accepted 22 January 1998

Open reading frame IV (ORF-IV) of Borna disease virus (BDV) encodes a protein with a calculated molecular mass of ca. 57 kDa (p57), which increases after N glycosylation to 94 kDa (gp94). The unglycosylated and glycosylated proteins are proteolytically cleaved by the subtilisin-like protease furin. Furin most likely recognizes one of three potential cleavage sites, namely, an arginine at position 249 of the ORF-IV gene product. The furin inhibitor decRVKRcmk decreases the production of infectious BDV significantly, indicating that proteolytic cleavage of the gp94 precursor molecule is necessary for the full biological activity of the BDV glycoprotein.

* Corresponding author. Mailing address: Institut für Virologie, Frankfurterstr. 107, D-35392 Giessen, Germany. Phone: (49) 641-99-38384. Fax: (49) 641-99-38359. E-mail: juergen.a.richt{at}vetmed.uni-giessen.de.

J Virol, May 1998, p. 4528-4533, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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