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Host-dependent phosphorylation and kinase activity associated with vesicular stomatitis virus
The Journal of Biological Chemistry
|March 25, 1982
Summary
Vesicular stomatitis virus (VSV) contains pp60src, a tyrosine kinase. Increasing pp60src activity enhances tyrosine phosphorylation of VSV M protein without altering other functions.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Vesicular stomatitis virus (VSV) is a model system for studying virus-host interactions.
- Protein kinases play crucial roles in viral replication and pathogenesis.
- pp60src is a known tyrosine kinase associated with viral transformation.
Purpose of the Study:
- To identify protein kinases associated with VSV.
- To investigate the role of pp60src in VSV infection and M protein phosphorylation.
- To determine if pp60src activity can be manipulated by host cell conditions.
Main Methods:
- Immunoprecipitation was used to identify protein kinases in VSV.
- Western blotting and kinase assays were performed to quantify pp60src activity.
- VSV was propagated in different host cells to manipulate pp60src content.
Main Results:
- pp60src, a tyrosine-specific kinase, was identified in VSV-associated proteins.
- Growing VSV in transformed baby hamster kidney cells increased pp60src activity by 7-fold.
- Increased pp60src specifically enhanced tyrosine phosphorylation of the VSV M protein up to 20-fold.
Conclusions:
- pp60src is a significant tyrosine kinase associated with VSV.
- The level of pp60src in VSV can be modulated by the host cell environment.
- pp60src-mediated tyrosine phosphorylation of the M protein does not appear to alter its function.