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Expression and processing of the canine calicivirus capsid precursor
1Laboratory of Veterinary Microbiology, Department of Veterinary Medicine, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065 Japan.
The Journal of General Virology
|January 21, 2000
Summary
The canine calicivirus (CaCV) ORF2 protein precursor is processed into mature capsid proteins by a feline calicivirus (FCV) proteinase. This suggests CaCV may possess a similar proteinase for its capsid maturation.
Area of Science:
- Virology
- Molecular Biology
Background:
- Canine calicivirus (CaCV) is a significant pathogen.
- Understanding the molecular mechanisms of viral capsid formation is crucial for developing antiviral strategies.
Purpose of the Study:
- To identify and analyze the processing of the canine calicivirus (CaCV) ORF2 product in mammalian cells.
- To investigate the role of proteinases in CaCV capsid maturation.
Main Methods:
- Immunoblot analysis of CaCV-infected cells and cells expressing CaCV ORF2.
- Co-expression of CaCV ORF2 with feline calicivirus (FCV) proteinase.
- Site-directed mutagenesis to identify the cleavage site.
Main Results:
- A 75 kDa capsid precursor, a 57 kDa capsid protein, and a 22 kDa N-terminal polypeptide were detected in CaCV-infected cells.
- In a transient mammalian expression system, only the 75 kDa precursor was observed.
- Co-expression with FCV proteinase resulted in processing of the CaCV precursor to 57 kDa and 22 kDa products.
- Mutagenesis of the putative cleavage site blocked this processing.
Conclusions:
- The feline calicivirus (FCV) proteinase can cleave the canine calicivirus (CaCV) capsid precursor.
- CaCV likely possesses a similar endogenous proteinase for its capsid maturation.