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Effect of poliovirus superinfection on Sendai virus protein synthesis
Abstract:
Poliovirus superinfection of Sendai virus-infected cells inhibited the syntheses of the structural P protein and the nonstructural C' and C proteins equally. As the Sendai virus P, C', and C proteins are all translated from the same mRNA by ribosomes which initiate on alternate AUGs and as non-poliovirus protein synthesis is inhibited in poliovirus-infected cells by inactivation of initiation factors responsible for cap group recognition, these results indicate that cap group recognition is important for ribosome initiation on AUGs which are not proximal to the 5' end of the mRNA.
Insights
Superinfection with poliovirus halts synthesis of Sendai virus proteins. This suggests cap recognition is crucial for ribosomes initiating translation on internal AUGs in mRNA.
Area of Science:
- Molecular Biology
- Virology
- Biochemistry
Background:
- Sendai virus encodes structural P and nonstructural C'/C proteins from a single mRNA.
- These proteins are translated via alternative initiation on AUG codons.
- Poliovirus infection inhibits host protein synthesis by targeting cap-dependent initiation factors.
Purpose of the Study:
- To investigate the effect of poliovirus superinfection on Sendai virus protein synthesis.
- To determine the role of cap recognition in internal AUG initiation during viral coinfection.
Main Methods:
- Cells were infected with Sendai virus and subsequently superinfected with poliovirus.
- Protein synthesis was analyzed to quantify the production of viral proteins.
Main Results:
- Poliovirus superinfection equally inhibited the synthesis of Sendai virus P, C', and C proteins.
- This inhibition occurred despite the proteins being translated from the same mRNA via alternative AUG initiation.
Conclusions:
- Cap recognition is essential for ribosome initiation at AUG codons not located at the 5' end of mRNA.
- Poliovirus's inhibition of cap-dependent factors impacts translation of non-poliovirus mRNAs with internal initiation sites.