Abstract
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.
MeSH Terms
Amino Acid Chloromethyl Ketones/pharmacology
Amino Acid Sequence
Animals
Borna disease virus/metabolism,physiology
Brain/metabolism
Cell Line
Chlorocebus aethiops
Furin
Glycoproteins/chemistry,metabolism
Glycosylation
Protein Processing, Post-Translational
Rats
Serine Proteinase Inhibitors/pharmacology
Subtilisins/metabolism
Viral Proteins/chemistry,metabolism
Chemicals
Amino Acid Chloromethyl Ketones
Glycoproteins
Serine Proteinase Inhibitors
Viral Proteins
Subtilisins
Furin
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Richt J A
Institut für Virologie, Giessen, Germany. juergen.a.richt@vetmed.uni-giessen.de
Fürbringer T
Koch A
Pfeuffer I
Herden C
Bause-Niedrig I
Garten W
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