The Amino-terminal Half of Sendai Virus C Protein is Not Responsible for Either Counteracting the Antiviral Action of Interferons or Down-regulating Viral RNA Synthesis
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The Sendai virus C proteins, C', C, Y1, and Y2, are a nested set of independently initiated carboxy-coterminal proteins translated from a reading frame overlapping the P frame on the P mRNA. The C proteins are extremely versatile and have been shown to counteract the antiviral action of interferons (IFNs), to down-regulate viral RNA synthesis, and to promote virus assembly. Using the stable cell lines expressing the C, Y1, Y2, or truncated C protein, we investigated the region responsible for anti-IFN action and for down-regulating viral RNA synthesis. Truncation from the amino terminus to the middle of the C protein maintained the inhibition of the signal transduction of IFNs, the formation of IFN-stimulated gene factor 3 (ISGF3) complex, the generation of the anti-vesicular stomatitis virus state, and the synthesis of viral RNA, but further truncation resulted in the simultaneous loss of all of these inhibitory activities. A relatively small truncation from the carboxy terminus also abolished all of these inhibitory activities. These data indicated that the activities of the C protein to counteract the antiviral action of IFNs and to down-regulate viral RNA synthesis were not encoded within a region of at least 98 amino acids in its amino-terminal half.
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Kiener R, Fleischmann M, Wiegand M, Lemmermann N, Schwegler C, Kaufmann C J Virol. 2018; 92(15).
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Structural Basis of the Inhibition of STAT1 Activity by Sendai Virus C Protein.
Oda K, Matoba Y, Irie T, Kawabata R, Fukushi M, Sugiyama M J Virol. 2015; 89(22):11487-99.
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Lo M, Sogaard T, Karlin D PLoS One. 2014; 9(2):e90003.
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