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Cleavage efficiency by adenovirus protease is site-dependent
M Diouri1, H Keyvani-Amineh, K F Geoghegan
1Department of Microbiology, Faculty of Medicine, University of Sherbrooke, Quebec, Canada J1H 5N4. j.weber@courrier.usherb.ca
The Journal of Biological Chemistry
|December 20, 1996
Summary
Adenovirus protease preferentially cleaves the GX-G sequence over the GG-X sequence. This differential cleavage efficiency on viral protein pVI suggests a specific biological role in adenovirus replication.
Area of Science:
- Virology
- Molecular Biology
- Enzymology
Background:
- Adenoviruses utilize a specific protease for viral maturation.
- This protease recognizes and cleaves consensus sequences within viral proteins.
- Two primary cleavage sites, (M/I/L)XGX-G and (M/I/L)XGG-X, have been identified.
Purpose of the Study:
- To investigate the substrate specificity of the adenovirus protease.
- To compare the cleavage efficiency of the GX-G and GG-X consensus sequences.
- To determine the biological relevance of differential cleavage efficiency.
Main Methods:
- Purification of recombinant adenovirus protease.
- Synthesis and use of peptides containing GX-G and GG-X cleavage sites.
- Analysis of viral protein pVI cleavage using purified protease.
Main Results:
- The adenovirus protease hydrolyzed peptides with the GX-G site more rapidly than those with the GG-X site.
- Preferential cleavage of the GX-G site was observed on viral protein pVI, which contains both sequences.
- Differential cleavage efficiency was demonstrated in vitro.
Conclusions:
- The adenovirus protease exhibits distinct substrate preferences for different consensus sequences.
- The GX-G sequence is a preferred cleavage site compared to GG-X.
- This differential cleavage likely plays a significant role in the adenovirus life cycle.