scholarly journals Dephosphorylation Failure of Tyrosine-Phosphorylated STAT1 in IFN-Stimulated Sendai Virus C Protein-Expressing Cells

Virology ◽  
2002 ◽  
Vol 293 (2) ◽  
pp. 205-209 ◽  
Author(s):  
Sakura Saito ◽  
Toshio Ogino ◽  
Naoko Miyajima ◽  
Atsushi Kato ◽  
Masayoshi Kohase
Keyword(s):  
Sendai Virus ◽  
C Protein ◽  
Virus C

scholarly journals Sendai virus C protein limits NO production in infected RAW264.7 macrophages

2018 ◽  
Vol 24 (7) ◽  
pp. 430-438 ◽  
Author(s):  
Erdenezaya Odkhuu ◽  
Takayuki Komatsu ◽  
Naoki Koide ◽  
Yoshikazu Naiki ◽  
Kenji Takeuchi ◽  
...  
Keyword(s):  
Sendai Virus ◽  
Virus Multiplication ◽  
Inos Expression ◽  
No Production ◽  
Ns1 Protein ◽  
Wild Type ◽  
C Protein ◽  
Raw264.7 Macrophages ◽  
Virus C ◽  
Stat Pathway

To suppress virus multiplication, infected macrophages produce NO. However, it remains unclear how infecting viruses then overcome NO challenge. In the present study, we report the effects of accessory protein C from Sendai virus (SeV), a prototypical paramyxovirus, on NO output. We found that in RAW264.7 murine macrophages, a mutant SeV without C protein (4C(–)) significantly enhanced inducible NO synthase (iNOS) expression and subsequent NO production compared to wild type SeV (wtSeV). SeV 4C(-) infection caused marked production of IFN-β, which is involved in induction of iNOS expression via the JAK-STAT pathway. Addition of anti-IFN-β Ab, however, resulted in only marginal suppression of NO production. In contrast, NF-κB, a primarily important factor for transcription of the iNOS gene, was also activated by 4C(–) infection but not wtSeV infection. Induction of NO production and iNOS expression by 4C(–) was significantly suppressed in cells constitutively expressing influenza virus NS1 protein that can sequester double-stranded (ds)RNA, which triggers activation of signaling pathways leading to activation of NF-κB and IRF3. Therefore, C protein appears to suppress NF-κB activation to inhibit iNOS expression and subsequent NO production, possibly by limiting dsRNA generation in the context of viral infection.

Sendai virus C protein physically associates with Stat1

2001 ◽  
Vol 6 (6) ◽  
pp. 545-557 ◽  
Author(s):  
Kenji Takeuchi ◽  
Takayuki Komatsu ◽  
Junko Yokoo ◽  
Atsushi Kato ◽  
Tatsuo Shioda ◽  
...  
Keyword(s):  
Sendai Virus ◽  
C Protein ◽  
Virus C

scholarly journals Targeting of the Sendai Virus C Protein to the Plasma Membrane via a Peptide-Only Membrane Anchor

2007 ◽  
Vol 81 (7) ◽  
pp. 3187-3197 ◽  
Author(s):  
Jean-Baptiste Marq ◽  
Albert Brini ◽  
Daniel Kolakofsky ◽  
Dominique Garcin
Keyword(s):  
Plasma Membrane ◽  
Sendai Virus ◽  
Intracellular Localization ◽  
Membrane Targeting ◽  
Membrane Anchor ◽  
C Protein ◽  
Cellular Antiviral Response ◽  
Α Helix ◽  
Virus C ◽  
Cellular Compartments

ABSTRACT Several cellular proteins are synthesized in the cytosol on free ribosomes and then associate with membranes due to the presence of short peptide sequences. These membrane-targeting sequences contain sites to which lipid chains are attached, which help direct the protein to a particular membrane domain and anchor it firmly in the bilayer. The intracellular concentration of these proteins in particular cellular compartments, where their interacting partners are also concentrated, is essential to their function. This paper reports that the apparently unmodified N-terminal sequence of the Sendai virus C protein (MPSFL KK IL K L R G RR . . .; letters in italics represent hydrophobic residues; underlined letters represent basic residues, which has a strong propensity to form an amphipathic α-helix in a hydrophobic environment) also function as a membrane targeting signal and membrane anchor. Moreover, the intracellular localization of the C protein at the plasma membrane is essential for inducing the interferon-independent phosphorylation of Stat1 as part of the viral program to prevent the cellular antiviral response.

Sendai virus C protein impairs both phosphorylation and dephosphorylation processes of Stat1

FEBS Letters ◽  
2002 ◽  
Vol 511 (1-3) ◽  
pp. 139-144 ◽  
Author(s):  
Takayuki Komatsu ◽  
Kenji Takeuchi ◽  
Junko Yokoo ◽  
Bin Gotoh
Keyword(s):  
Sendai Virus ◽  
C Protein ◽  
Virus C

Sendai virus C protein inhibits lipopolysaccharide-induced nitric oxide production through impairing interferon-β signaling

2014 ◽  
Vol 23 (1) ◽  
pp. 267-272 ◽  
Author(s):  
Erdenezaya Odkhuu ◽  
Takayuki Komatsu ◽  
Yoshikazu Naiki ◽  
Naoki Koide ◽  
Takashi Yokochi
Keyword(s):  
Nitric Oxide ◽  
Sendai Virus ◽  
Nitric Oxide Production ◽  
Interferon Β ◽  
C Protein ◽  
Oxide Production ◽  
Virus C

scholarly journals Sendai Virus C Proteins Counteract the Interferon-Mediated Induction of an Antiviral State

1999 ◽  
Vol 73 (8) ◽  
pp. 6559-6565 ◽  
Author(s):  
Dominique Garcin ◽  
Patrizia Latorre ◽  
Daniel Kolakofsky
Keyword(s):  
Sendai Virus ◽  
Antiviral Response ◽  
Single Amino Acid ◽  
Wild Type ◽  
C Protein ◽  
Antiviral State ◽  
Protein Levels ◽  
Vesicular Stomatitis ◽  
C Proteins ◽  
Virus C

ABSTRACT We have studied the relationship between the Sendai virus (SeV) C proteins (a nested set of four proteins initiated at different start codons) and the interferon (IFN)-mediated antiviral response in IFN-competent cells in culture. SeV strains containing wild-type or various mutant C proteins were examined for their ability (i) to induce an antiviral state (i.e., to prevent the growth of vesicular stomatitis virus [VSV] following a period of SeV infection), (ii) to induce the elevation of Stat1 protein levels, and (iii) to prevent IFN added concomitant with the SeV infection from inducing an antiviral state. We find that expression of the wild-type C gene and, specifically, the AUG114-initiated C protein prevents the establishment of an antiviral state: i.e., cells infected with wild-type SeV exhibited little or no increase in Stat1 levels and were permissive for VSV replication, even in the presence of exogenous IFN. In contrast, in cells infected with SeV lacking the AUG114-initiated C protein or containing a single amino acid substitution in the C protein, the level of Stat1 increased and VSV replication was inhibited. The prevention of the cellular IFN-mediated antiviral response appears to be a key determinant of SeV pathogenicity.

Association of the Sendai virus C protein with nucleocapsids

1990 ◽  
Vol 113-113 (3-4) ◽  
pp. 245-253 ◽  
Author(s):  
H. Yamada ◽  
S. Hayata ◽  
T. Omata-Yamada ◽  
H. Taira ◽  
K. Mizumoto ◽  
...  
Keyword(s):  
Sendai Virus ◽  
C Protein ◽  
Virus C

scholarly journals Conserved Charged Amino Acids within Sendai Virus C Protein Play Multiple Roles in the Evasion of Innate Immune Responses

PLoS ONE ◽  
2010 ◽  
Vol 5 (5) ◽  
pp. e10719 ◽  
Author(s):  
Takashi Irie ◽  
Natsuko Nagata ◽  
Tomoki Igarashi ◽  
Isao Okamoto ◽  
Takemasa Sakaguchi
Keyword(s):  
Amino Acids ◽  
Immune Responses ◽  
Sendai Virus ◽  
Innate Immune ◽  
Multiple Roles ◽  
Innate Immune Responses ◽  
C Protein ◽  
Charged Amino Acids ◽  
Virus C
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