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.

journal_name

Virology

journal_title

Virology

authors

Volchkov VE,Volchkova VA,Ströher U,Becker S,Dolnik O,Cieplik M,Garten W,Klenk HD,Feldmann H

doi

10.1006/viro.1999.0110

subject

Has Abstract

pub_date

2000-03-01 00:00:00

pages

1-6

issue

1

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(99)90110-1

journal_volume

268

pub_type

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