Hepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity: mutagenic analysis of residues within the SH3 domain that contribute to the interaction
2008
HCV NS5A Protein Binds to Fyn Tyrosine Kinase
publication
Evidence: high
Author Information
Author(s): Shelton Holly, Harris Mark
Primary Institution: University of Leeds
Hypothesis
How does the hepatitis C virus NS5A protein interact with the SH3 domain of the Fyn tyrosine kinase?
Conclusion
The NS5A protein binds to the Fyn SH3 domain with high affinity, suggesting it can compete with other ligands in infected cells.
Supporting Evidence
- NS5A binds to the Fyn SH3 domain with a KD of 629 nM.
- The interaction does not require the presence of domain I of NS5A.
- Mutagenic analysis identified key residues in the Fyn SH3 domain that are critical for binding.
Takeaway
The NS5A protein from the hepatitis C virus can stick to a part of a protein called Fyn, which might help the virus do its job inside cells.
Methodology
The study involved expressing truncated forms of NS5A in E. coli and analyzing their binding to the Fyn SH3 domain using surface plasmon resonance.
Digital Object Identifier (DOI)
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