» Articles » PMID: 12072511

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

Overview
Journal J Virol
Date 2002 Jun 20
PMID 12072511
Citations 20
Authors
Affiliations
Soon will be listed here.
Abstract

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.

Citing Articles

C Proteins: Controllers of Orderly Paramyxovirus Replication and of the Innate Immune Response.

Siering O, Cattaneo R, Pfaller C Viruses. 2022; 14(1).

PMID: 35062341 PMC: 8778822. DOI: 10.3390/v14010137.


C Protein is Essential for Canine Distemper Virus Virulence and Pathogenicity in Ferrets.

Siering O, Sawatsky B, Pfaller C J Virol. 2020; 95(4).

PMID: 33239455 PMC: 7851556. DOI: 10.1128/JVI.01840-20.


Efficient Delivery of Human Cytomegalovirus T Cell Antigens by Attenuated Sendai Virus Vectors.

Kiener R, Fleischmann M, Wiegand M, Lemmermann N, Schwegler C, Kaufmann C J Virol. 2018; 92(15).

PMID: 29769344 PMC: 6052310. DOI: 10.1128/JVI.00569-18.


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.

PMID: 26339056 PMC: 4645678. DOI: 10.1128/JVI.01887-15.


Evolution and structural organization of the C proteins of paramyxovirinae.

Lo M, Sogaard T, Karlin D PLoS One. 2014; 9(2):e90003.

PMID: 24587180 PMC: 3934983. DOI: 10.1371/journal.pone.0090003.


References
1.
Gotoh B, Takeuchi K, Komatsu T, Yokoo J, Kimura Y, Kurotani A . Knockout of the Sendai virus C gene eliminates the viral ability to prevent the interferon-alpha/beta-mediated responses. FEBS Lett. 1999; 459(2):205-10. DOI: 10.1016/s0014-5793(99)01241-7. View

2.
GARCIN D, Itoh M, Kolakofsky D . A point mutation in the Sendai virus accessory C proteins attenuates virulence for mice, but not virus growth in cell culture. Virology. 1997; 238(2):424-31. DOI: 10.1006/viro.1997.8836. View

3.
Didcock L, Young D, Goodbourn S, Randall R . The V protein of simian virus 5 inhibits interferon signalling by targeting STAT1 for proteasome-mediated degradation. J Virol. 1999; 73(12):9928-33. PMC: 113042. DOI: 10.1128/JVI.73.12.9928-9933.1999. View

4.
Patterson J, Thomas D, Lewicki H, Billeter M, Oldstone M . V and C proteins of measles virus function as virulence factors in vivo. Virology. 2000; 267(1):80-9. DOI: 10.1006/viro.1999.0118. View

5.
Komatsu T, Takeuchi K, Yokoo J, Tanaka Y, Gotoh B . Sendai virus blocks alpha interferon signaling to signal transducers and activators of transcription. J Virol. 2000; 74(5):2477-80. PMC: 111735. DOI: 10.1128/jvi.74.5.2477-2480.2000. View