The C-terminal half-fragment of the Sendai virus C protein prevents the gamma-activated factor from binding to a gamma-activated sequence site.
Sendai virus C protein associates with the signal transducer and activator of transcription (STAT) 1 and inhibits the interferon (IFN) response. We report a molecular basis for the anti-IFN-gamma mechanism of Sendai virus. The C-terminal half-fragment of the C protein (D1) retains both the STAT1-binding and the anti-IFN-gamma abilities comparable to those of the full-size C. IFN-gamma stimulation generates phosphorylated-STAT1 even in the presence of the C or the D1. The phosphorylated-STAT1 generated in the D1-expressing cells forms an aberrant complex, which does not bind to a gamma-activated sequence (GAS) probe. Purified D1, indeed, inhibits in vitro the binding of the phosphorylated-STAT1 dimer to the GAS probe. The D1, however, binds to the STAT1 N-terminal domain, but not the DNA binding domain. These results suggest the possibility that the C protein prevents the gamma- activated factor from binding to GAS elements through its interaction with the STAT1 N-terminal domain.[1]References
- The C-terminal half-fragment of the Sendai virus C protein prevents the gamma-activated factor from binding to a gamma-activated sequence site. Gotoh, B., Komatsu, T., Takeuchi, K., Yokoo, J. Virology (2003) [Pubmed]
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