Paramyxovirus strategies for evading the interferon response

Gotoh, Bin; Komatsu, Takayuki; Takeuchi, Kenji; Yokoo, Junko

doi:10.1002/rmv.357

Cited by 120 publications

(101 citation statements)

References 190 publications

(241 reference statements)

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“…In concordance with a type I IFN-independent induction of DC maturation, these viruses encode four proteins, C, CЈ, Y1, and Y2, collectively known as the C proteins, that are able to interfere with the signaling necessary for the responsiveness to type I IFNs (29,30). Accordingly, the phosphorylation of STAT1, an essential step in type I IFN signaling, is similarly inhibited by SeV-C and SeV-52 (Fig.…”

Section: Strong DC Maturation By Sev-c Is Not Antagonized By a Sev Wimentioning

confidence: 97%

A Novel Role for Viral-Defective Interfering Particles in Enhancing Dendritic Cell Maturation

Yount

Kraus

Horvath

et al. 2006

The Journal of Immunology

109

152

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Dendritic cell (DC) maturation is a crucial event in the development of adaptive immune responses that confer long-lasting protection against reinfection with the same virus. Sendai virus strain Cantell has a particularly strong ability to mature DCs independently of type I IFNs and TLR signaling, currently the best-described pathways for the induction of DC maturation. In this study, we demonstrate that defective-interfering (DI) particles present in Sendai virus-Cantell stocks are required for its robust DC maturation ability. DI particles contain incomplete genomes that are unable to replicate unless the viral polymerase is supplied by coinfection with complete virus. Accordingly, the improvement in the virus-induced maturation of DCs provided by DI particles requires standard virus coinfection and likely results from increased production of dsRNA replication intermediaries. This unique ability of DI particles to stimulate DC maturation cannot be mimicked by simply increasing the dose of standard virus. Furthermore, viruses with weak DC maturation abilities can be converted into potent DC stimulators with the addition of DI particles, supporting a potential application for DI particles as a novel natural adjuvant for viral immunizations.

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Section: Strong DC Maturation By Sev-c Is Not Antagonized By a Sev Wimentioning

confidence: 97%

A Novel Role for Viral-Defective Interfering Particles in Enhancing Dendritic Cell Maturation

Yount

Kraus

Horvath

et al. 2006

The Journal of Immunology

109

152

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“…Viruses have developed a wide range of mechanisms for inhibiting IFN␥ signaling, including production of decoy receptors and dominant negative intermediates (32). Of particular interest, paramyxovirus-encoded proteins have been shown to cause specific degradation of STAT1 by the proteasome by recruiting a cellular E3-ubiquitin-protein isopeptide ligase (33)(34)(35).…”

mentioning

confidence: 99%

Proteasome-mediated Degradation of STAT1α following Infection of Macrophages with Leishmania donovani

Forget

Gregory

Olivier

2005

Journal of Biological Chemistry

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Activation of the Janus-activated kinase 2 (JAK2)/ STAT1␣ signaling pathway is repressed in Leishmaniainfected macrophages. This represents an important mechanism by which this parasite subverts the microbicidal functions of the cell to promote its own survival and propagation. We recently provided evidence that the protein tyrosine phosphatase (PTP) SHP-1 was responsible for JAK2 inactivation. However, STAT1 translocation to the nucleus was not restored in the absence of SHP-1. In the present study, we have used B10R macrophages to study the mechanism by which this Leishmania-induced STAT1 inactivation occurs. STAT1␣ nuclear localization was shown to be rapidly reduced by the infection. Western blot analysis revealed that cellular STAT1␣, but not STAT3, was degraded. Using PTP inhibitors and an immortalized bone marrowderived macrophage cell line from SHP-1-deficient mice, we showed that STAT1 inactivation was independent of PTP activity. However, inhibition of macrophage proteasome activity significantly rescued Leishmania-induced STAT1␣ degradation. We further demonstrated that degradation was receptor-mediated and involved protein kinase C␣. All Leishmania species tested (L. major, L. donovani, L. mexicana, L. braziliensis), but not the related parasite Trypanosoma cruzi, caused STAT1␣ degradation. Collectively, results from this study revealed a new mechanism for STAT1 regulation by a microbial pathogen, which favors its establishment and propagation within the host.

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“…After stimulation with IFN-␥, ␥-activated factor, which is a dimer of phosphorylated STAT-1, binds to the ␥ activation sequence. Many viruses, for example those belonging to family Paramyxoviridae (12,13), are reported to shut off or suppress the IFN signaling pathway (8,9). Viruses belonging to the genus Respirovirus within the family Paramyxoviridae, such as Sendai virus and human parainfluenza virus type 3, reduce the Tyr phosphorylation of STAT-1 (14 -17).…”

mentioning

confidence: 99%

Suppression of Thermotolerance in Mumps Virus-infected Cells Is Caused by Lack of HSP27 Induction Contributed by STAT-1

Yokota

Yokosawa

Kubota

et al. 2003

Journal of Biological Chemistry

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Viral infection modulates the regulation of apoptosis in host cells. Here, we report a novel mechanism by which human cells infected with mumps virus become susceptible to apoptosis caused by extracellular stresses. Mumps virus stimulates proteasome-dependent degradation of STAT-1 by action of viral accessory protein V, resulting in a severe decrease in STAT-1 protein in infected cells. We exposed mumps virus-infected and uninfected cells to heat and chemical stress. The infected cells failed to acquire resistance to apoptotic stimuli (thermotolerance) after exposure to these mild stresses. The induction of HSP27 by stress exposure was dramatically suppressed in the infected cells, but HSP70 induction was not affected. STAT-1 was required for transcriptional activation of the HSP27 gene, but not for the HSP70 gene, and cDNA transfection of STAT-1 in mumps virus-infected cells restored thermotolerance. Phosphorylated heat shock factor-1 (HSF-1) and STAT-1 phosphorylated on neither tyrosine nor serine residues were co-transported to the nucleus in response to stress. Furthermore, overexpression of unphosphorylatable mutants of STAT-1 also restored thermotolerance in mumps virus-infected cells. These lines of evidence indicate that the induction of HSP27 by stress requires STAT-1 in addition to the activated HSF-1. Furthermore, STAT-1 required for the induction of HSP27 worked independent to its phosphorylation. Thus, HSP27-dependent thermotolerance is suppressed by mumps virus infection through the destruction of STAT-1. The lack of thermotolerance should allow the infected cells to be eliminated by apoptosis and might be a host defense against viral infection.

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Paramyxovirus strategies for evading the interferon response

Cited by 120 publications

References 190 publications

A Novel Role for Viral-Defective Interfering Particles in Enhancing Dendritic Cell Maturation

A Novel Role for Viral-Defective Interfering Particles in Enhancing Dendritic Cell Maturation

Proteasome-mediated Degradation of STAT1α following Infection of Macrophages with Leishmania donovani

Suppression of Thermotolerance in Mumps Virus-infected Cells Is Caused by Lack of HSP27 Induction Contributed by STAT-1

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