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PMID: 9557754 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Processing of the Borna disease virus glycoprotein gp94 by the subtilisin-like endoprotease furin.

Journal of virology ·Vol. 72 ·No. 5 ·1998-05-00 ·Pages 4528-33

Richt JA, Fürbringer T, Koch A, Pfeuffer I, Herden C, Bause-Niedrig I, Garten W

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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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1998-05-00
Pages
4528-33
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC109700
Subset
IM
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