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Proteolytic processing of Marburg virus glycoprotein
V E Volchkov1, V A Volchkova, U Ströher
1Institut für Virologie, Philipps-Universität, Robert-Koch-Str. 17, Marburg, D-35037, Germany. volchkov@mailer.uni-marburg.de
Virology
|February 23, 2000
Summary
Marburg virus glycoprotein (GP) processing involves endo H-sensitive ER forms converting to endo H-resistant Golgi precursors, then cleaved into GP(1) and GP(2) subunits by furin or similar proteases.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- The Marburg virus glycoprotein (GP) is crucial for viral entry and pathogenesis.
- Understanding GP processing is key to developing antiviral strategies.
Purpose of the Study:
- To elucidate the post-translational modification and processing pathway of the Marburg virus glycoprotein (GP).
- To identify the specific proteases responsible for GP cleavage.
Main Methods:
- Endo H sensitivity assays to track glycoprotein maturation.
- Mutational analysis of the GP cleavage site.
- Inhibition studies using peptidyl chloromethylketones.
Main Results:
- Marburg virus GP undergoes conversion from an endo H-sensitive, ER-specific form to an endo H-resistant, Golgi-specific precursor.
- This precursor is subsequently cleaved into mature GP(1) and GP(2) subunits.
- Cleavage is mediated by furin or a related subtilisin-like endoprotease, confirmed by mutational analysis and protease inhibitors.
Conclusions:
- The processing of Marburg virus GP is a multi-step pathway involving intracellular transport and proteolytic cleavage.
- Furin or a similar protease is essential for generating the functional subunits of Marburg virus GP.