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Journal of Virology, July 2002, p. 7114-7124, Vol. 76, No. 14
0022-538X/02/$04.00+0 DOI: 10.1128/JVI.76.14.7114-7124.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Department of Viral Diseases and Vaccine Control, National Institute of Infectious Diseases, Musashi-Murayama, Tokyo 208-0011,1 Bio-Oriented Technology Research Advancement Institution (BRAIN), Saitama 331-8537,2 Toyama Institute of Health, Kosugi-machi, Toyama 939-0363, Japan3
Received 17 January 2002/ Accepted 22 April 2002
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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