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Substrate specificity of adenovirus protease
Angelique Ruzindana-Umunyana1, Lise Imbeault, Joseph M Weber
1Département de Microbiologie et d'Infectiologie, Faculté de Médecine, Université de Sherbrooke, Sherbrooke, Québec, Canada J1H 5N4.
Virus Research
|October 9, 2002
Summary
Adenovirus protease (adenain) cleaves viral proteins. While it prefers consensus sites, it can also cut at other specific locations, aiding in virus uncoating and maturation.
Area of Science:
- Virology
- Molecular Biology
- Structural Biology
Background:
- Adenovirus protease (adenain) is crucial for viral replication, involved in virion uncoating, maturation, and release.
- Adenain hydrolyzes precursor proteins at specific consensus sites, but also cleaves viral proteins at non-consensus sites.
Purpose of the Study:
- To re-examine adenovirus protease consensus cleavage sites.
- To investigate the cleavage of viral proteins at non-consensus sites by adenain.
Main Methods:
- Analysis of 274 consensus sites from 36 adenovirus serotypes in DNA sequence databases.
- In vitro cleavage assays using recombinant adenain on viral proteins II, 100K, V, VI, and VII.
Main Results:
- Identified two types of adenain consensus sites: (M,I,L)XGX-G and (M,I,L)XGG-X.
- Defined amino acid restrictions at variant positions within consensus sites.
- Confirmed in vitro cleavage of capsid protein VI at a non-consensus site.
- Demonstrated adenain's ability to fragment multiple viral proteins (II, 100K, V, VII) in vitro.
Conclusions:
- Adenain preferentially cleaves viral proteins at consensus sites.
- Adenain exhibits broader cleavage activity, cutting at other discrete sites resembling consensus sequences.
- This dual cleavage capability contributes to adenovirus virion uncoating and maturation processes.