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.
journal_name
Virologyjournal_title
Virologyauthors
Volchkov VE,Volchkova VA,Ströher U,Becker S,Dolnik O,Cieplik M,Garten W,Klenk HD,Feldmann Hdoi
10.1006/viro.1999.0110subject
Has Abstractpub_date
2000-03-01 00:00:00pages
1-6issue
1eissn
0042-6822issn
1096-0341pii
S0042-6822(99)90110-1journal_volume
268pub_type
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