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Adenovirus assembly: self-assembly of partially digested hexons.
Journal of Virology
|December 1, 1975
Summary
Papainic hydrolysis of adenovirus type 2 hexon capsomers yielded trimers that retained immunological properties. These trimers aggregated, suggesting a role in adenovirus assembly.
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- Adenovirus capsomers are essential for viral structure.
- Understanding hexon behavior is key to viral assembly insights.
Purpose of the Study:
- To investigate the effects of papainic hydrolysis on adenovirus type 2 hexon capsomers.
- To characterize the resulting oligomeric species and their properties.
Main Methods:
- Limited papainic hydrolysis of hexon capsomers.
- Sedimentation analysis to determine oligomeric species.
- Assessment of immunological properties.
Main Results:
- Hydrolysis induced self-aggregation of hexons into preferred oligomeric species, specifically hexon trimers.
- These hexon trimers sedimented at approximately 19S.
- The trimers maintained their original immunological characteristics.
- Two classes of trimer molecules with distinct electric charges were identified.
Conclusions:
- Papainic hydrolysis leads to the formation of stable hexon trimers from adenovirus type 2 capsomers.
- The observed trimer aggregation phenomenon may be relevant to the in vivo assembly process of adenoviruses.
- Hexon trimers represent a significant oligomeric state in adenovirus assembly.