title: Proteolytic processing of Marburg virus glycoprotein.
abstract: 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.
authors.affiliation: Institut für Virologie, Philipps-Universität, Robert-Koch-Str. 17, Marburg, D-35037, Germany. volchkov@mailer.uni-marburg.de
authors.forename: V E
authors.initials: VE
authors.lastname: Volchkov
authors.forename: V A
authors.initials: VA
authors.lastname: Volchkova
authors.forename: U
authors.initials: U
authors.lastname: Ströher
authors.forename: S
authors.initials: S
authors.lastname: Becker
authors.forename: O
authors.initials: O
authors.lastname: Dolnik
authors.forename: M
authors.initials: M
authors.lastname: Cieplik
authors.forename: W
authors.initials: W
authors.lastname: Garten
authors.forename: H D
authors.initials: HD
authors.lastname: Klenk
authors.forename: H
authors.initials: H
authors.lastname: Feldmann
mesh_terms: 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*
chemical_list: C081324:GP-protein, Marburg virus; D014759:Viral Envelope Proteins; D013381:Subtilisins; D045683:Furin