Proteolytic processing of Marburg virus glycoprotein.
Processing of the transmembrane glycoprotein (GP) of Marburg virus involved the conversion of an endo H-sensitive, ER-specific form into an endo H-resistant, Golgi-specific precursor that was cleaved into GP(1) and GP(2). Cleavage was mediated by furin or another subtilisin-like endoprotease with similar substrate specificity as indicated by mutational analysis of the cleavage site and inhibition using peptidyl chloromethylketones. Mature GP consisted of disulfide-linked GP(1) and GP(2) subunits.
Volchkov
V E
VE
Institut für Virologie, Philipps-Universität, Robert-Koch-Str. 17, Marburg, D-35037, Germany. volchkov@mailer.uni-marburg.de
Volchkova
V A
VA
Ströher
U
U
Becker
S
S
Dolnik
O
O
Cieplik
M
M
Garten
W
W
Klenk
H D
HD
Feldmann
H
H
D000818:Animals; D002522:Chlorocebus aethiops; D045683:Furin; D006367:HeLa Cells; D006801:Humans; D029024:Marburgvirus / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D011499:Protein Processing, Post-Translational; D013381:Subtilisins / Q000378:metabolism; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000235:genetics* / Q000378:metabolism*
C081324:GP-protein, Marburg virus; D014759:Viral Envelope Proteins; D013381:Subtilisins; D045683:Furin