Peroxiredoxin 1 Is Required for Efficient Transcription and Replication of Measles Virus

Watanabe, Akira; Yoneda, Misako; Ikeda, Fusako; Sugai, Akihiro; Sato, Hiroki; Cui, Kai

doi:10.1128/jvi.01796-10

Cited by 34 publications

(24 citation statements)

References 33 publications

(37 reference statements)

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“…Cyclophilin A binds to the N protein and is a required factor for replication of VSV NJ but not VSV I (10). Recently, peroxiredoxin 1 was identified as a binding partner of the nucleocapsid protein of measles virus and was found to be required for its replication and transcription (63). Hantavirus nucleocapsid protein binds to a ribosomal protein, RPS19, and mediates preferential translation of viral mRNA (14).…”

Section: Discussionmentioning

confidence: 99%

Antagonistic Effects of Cellular Poly(C) Binding Proteins on Vesicular Stomatitis Virus Gene Expression

Dinh

Beura

Panda³

et al. 2011

J Virol

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Immunoprecipitation and subsequent mass spectrometry analysis of the cellular proteins from cells expressing the vesicular stomatitis virus (VSV) P protein identified the poly(C) binding protein 2 (PCBP2) as one of the P protein-interacting proteins. To investigate the role of PCBP2 in the viral life cycle, we examined the effects of depletion or overexpression of this protein on VSV growth. Small interfering RNA-mediated silencing of PCBP2 promoted VSV replication. Conversely, overexpression of PCBP2 in transfected cells suppressed VSV growth. Further studies revealed that PCBP2 negatively regulates overall viral mRNA accumulation and subsequent genome replication. Coimmunoprecipitation and immunofluorescence microscopic studies showed that PCBP2 interacts and colocalizes with VSV P protein in virus-infected cells. The P-PCBP2 interaction did not result in reduced levels of protein complex formation with the viral N and L proteins, nor did it induce degradation of the P protein. In addition, PCBP1, another member of the poly(C) binding protein family with homology to PCBP2, was also found to interact with the P protein and inhibit the viral mRNA synthesis at the level of primary transcription without affecting secondary transcription or genome replication. The inhibitory effects of PCBP1 on VSV replication were less pronounced than those of PCBP2. Overall, the results presented here suggest that cellular PCBP2 and PCBP1 antagonize VSV growth by affecting viral gene expression and highlight the importance of these two cellular proteins in restricting virus infections. Vesicular stomatitis virus (VSV)is an enveloped RNA virus in the family Rhabdoviridae. The negative-sense RNA genome of VSV is 11,161 nucleotides in length and encodes 5 proteins: the nucleocapsid protein (N), the phosphoprotein (P), the matrix (M), the glycoprotein (G), and the large protein (L). Inside the virion, the viral genome is tightly encapsidated with the N protein to form the ribonucleocapsid complex (RNP or NC) with which the viral RNA-dependent RNA polymerase (RdRp) complex of P-L proteins (41) is associated. The G protein forms spikes on the surface of the VSV virion and mediates virus attachment as well as entry by clathrin-mediated endocytosis. Based on the low-pH environment of the endosome, the VSV G protein mediates fusion of the viral envelope with the endosomal membrane, releasing the viral RNP into the cytoplasm of the infected cell. Once inside the cytosol, the RNP undergoes primary transcription by the associated RdRp activity of the L protein along with its cofactor P protein. Translation of the transcripts by the cellular translation machinery generates viral proteins, which are used for further steps in the infection process, including genome replication, secondary transcription, assembly, and budding (53).The viral P is a multifunctional protein that modulates the association of viral replicative proteins and is indispensable for viral growth. It is required for viral genome transcription and replication (18) and also pl...

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Section: Discussionmentioning

confidence: 99%

Antagonistic Effects of Cellular Poly(C) Binding Proteins on Vesicular Stomatitis Virus Gene Expression

Dinh

Beura

Panda³

et al. 2011

J Virol

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“…promiscuity) [90]. In fact, in addition to P, MeV N TAIL does also interact with the M protein [91] and many cellular proteins [49,50,77,[92][93][94][95][96], which leads to plethora of functional effects including virus assembly, stimulation of transcription and replication, and evasion of the antiviral response. The presence of long disordered regions is not unique to paramyxoviral N proteins, being also a conserved property of P proteins of Paramyxovirinae members [28,97,98].…”

Section: Functional Impact Of the N Tail -Xd Interaction And Of Strucmentioning

confidence: 99%

Structural disorder within paramyxoviral nucleoproteins

Longhi

2015

FEBS Letters

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In this review I summarize available data pointing to the abundance of structural disorder within the nucleoprotein (N) from three paramyxoviruses, namely the measles (MeV), Nipah (NiV) and Hendra (HeV) viruses. I provide a detailed description of the molecular mechanisms that govern the disorder-to-order transition that the intrinsically disordered C-terminal domain (NTAIL) of their N proteins undergoes upon binding to the C-terminal X domain (XD) of the homologous phosphoproteins. I also show that a significant flexibility persists within NTAIL-XD complexes, which makes them illustrative examples of "fuzziness". Finally, I discuss the functional implications of structural disorder for viral transcription and replication in light of the promiscuity of disordered regions and of the considerable reach they confer to the components of the replicative machinery.

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“…(79) It was shown Prx1 binds to the C-terminal region of the nucleoprotein (NTAIL) of the virus and enhance RNA synthesis of the virus in the cells.…”

Section: Biological Functions Of Extracellular Prxsmentioning

confidence: 99%

Novel roles of peroxiredoxins in inflammation, cancer and innate immunity

Ishii

Warabi

Yanagawa

2012

J. Clin. Biochem. Nutr.

129

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Peroxiredoxins possess thioredoxin or glutathione peroxidase and chaperone-like activities and thereby protect cells from oxidative insults. Recent studies, however, reveal additional functions of peroxiredoxins in gene expression and inflammation-related biological reactions such as tissue repair, parasite infection and tumor progression. Notably, peroxiredoxin 1, the major mammalian peroxiredoxin family protein, directly interacts with transcription factors such as c-Myc and NF-κB in the nucleus. Additionally, peroxiredoxin 1 is secreted from some cells following stimulation with TGF-β and other cytokines and is thus present in plasma and body fluids. Peroxiredoxin 1 is now recognized as one of the pro-inflammatory factors interacting with toll-like receptor 4, which triggers NF-κB activation and other signaling pathways to evoke inflammatory reactions. Some cancer cells release peroxiredoxin 1 to stimulate toll-like receptor 4-mediated signaling for their progression. Interestingly, peroxiredoxins expressed in protozoa and helminth may modulate host immune responses partly through toll-like receptor 4 for their survival and progression in host. Extracellular peroxiredoxin 1 and peroxiredoxin 2 are known to enhance natural killer cell activity and suppress virus-replication in cells. Peroxiredoxin 1-deficient mice show reduced antioxidant activities but also exhibit restrained tissue inflammatory reactions under some patho-physiological conditions. Novel functions of peroxiredoxins in inflammation, cancer and innate immunity are the focus of this review.

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Peroxiredoxin 1 Is Required for Efficient Transcription and Replication of Measles Virus

Cited by 34 publications

References 33 publications

Antagonistic Effects of Cellular Poly(C) Binding Proteins on Vesicular Stomatitis Virus Gene Expression

Antagonistic Effects of Cellular Poly(C) Binding Proteins on Vesicular Stomatitis Virus Gene Expression

Structural disorder within paramyxoviral nucleoproteins

Novel roles of peroxiredoxins in inflammation, cancer and innate immunity

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