Rinderpest Virus C and V Proteins Interact with the Major (L) Component of the Viral Polymerase

Sweetman, David A.; Miskin, James; Baron, Michael D.

doi:10.1006/viro.2000.0805

Cited by 39 publications

(31 citation statements)

References 80 publications

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“…3a). STAT1 was found to colocalize with the viral P protein (and therefore also with the viral N, L, C, and possibly V proteins [70]) (Fig. 3a).…”

Section: Resultsmentioning

confidence: 99%

“…Rabbit polyclonal antibody against green fluorescent protein was from Abcam. Rabbit polyclonal antibodies against RPV P (MB18), N (MB2), and C (MB36) proteins were previously prepared in our lab (4,70). Mouse monoclonal antibodies (U32) (against an epitope common to RPV P and V proteins) and 2-1 (recognizing specifically the RPV P protein) were the kind gift of M. Sugiyama, Department of Veterinary Public Health, Faculty of Agriculture, Gifu University, Gifu, Japan (69 Virus infection, IFN treatment, cell extraction, and immunoblotting.…”

Section: Methodsmentioning

confidence: 99%

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Rinderpest Virus Blocks Type I and Type II Interferon Action: Role of Structural and Nonstructural Proteins

Nanda

Baron

2006

J Virol

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Rinderpest virus (RPV) is a paramyxovirus closely related to the human pathogen Measles virus. It causes severe disease in cattle, buffalo, and some wild animals; although it can infect humans, it does not cause disease. Here, we demonstrate that RPV blocks the action of both type I (␣) and type II (␥) interferons (IFNs) by blocking the phosphorylation and nuclear translocation of STAT1 and STAT2 and that this block is not related to species specificity. In addition, both wild-type virulent and vaccine strains of the virus blocked IFN action. Unlike the case with some other paramyxoviruses, neither STAT1 nor STAT2 is degraded upon virus infection. STAT1 is bound by both the viral structural protein P, and thereby recruited to concentrations of viral protein in the cell, and the nonstructural protein V. Although both P and V proteins bind to STAT1 and can block IFN action when expressed in transfected cells, the IFN antagonist activity of the P protein is weaker than that of the V protein. The viral C protein also seems to weakly block IFN-induced activation of STAT1 in transfection experiments. However, studies with knockout viruses showed that the viral V protein appears to be the dominant inhibitor of IFN signaling in the context of virus infection, since prevention of viral V expression restored the IFN sensitivity of infected cells. Although a change in the distribution pattern of STAT2 was observed in virus-infected cells, STAT2 was not bound by any viral protein.

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“…3a). STAT1 was found to colocalize with the viral P protein (and therefore also with the viral N, L, C, and possibly V proteins [70]) (Fig. 3a).…”

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Rinderpest Virus Blocks Type I and Type II Interferon Action: Role of Structural and Nonstructural Proteins

Nanda

Baron

2006

J Virol

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“…In addition, the V protein of SeV inhibited the replication of defective interfering particles (Curran et al, 1991;Horikami et al, 1996), and the V protein of SV5 inhibited viral transcription and replication (Lin et al, 2005). For a number of paramyxoviruses, it has been postulated that the mechanism by which V controls viral replication may be through a direct protein-protein interaction with the nucleocapsid (N) protein (Curran et al, 1991;Horikami et al, 1996;Lin et al, 2005;Svenda et al, 2002;Sweetman et al, 2001). However, recent studies with the V protein of MV discounted the possibility that a V-N interaction is responsible for the inhibitory effect .…”

Section: Discussionmentioning

confidence: 99%

The C, V and W proteins of Nipah virus inhibit minigenome replication

Sleeman

Bankamp

Hummel

et al. 2008

Journal of General Virology

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Nipah virus (NiV) is a recently emergent, highly pathogenic, zoonotic paramyxovirus of the genus Henipavirus. Like the phosphoprotein (P) gene of other paramyxoviruses, the P gene of NiV is predicted to encode three additional proteins, C, V and W. When the C, V and W proteins of NiV were tested for their ability to inhibit expression of the chloramphenicol acetyltransferase (CAT) reporter gene in plasmid-based, minigenome replication assays, each protein inhibited CAT expression in a dose-dependent manner. The C, V and W proteins of NiV also inhibited expression of CAT from a measles virus (MV) minigenome, but not from a human parainfluenzavirus 3 (hPIV3) minigenome. Interestingly, the C and V proteins of MV, which have previously been shown to inhibit MV minigenome replication, also inhibited NiV minigenome replication; however, they were not able to inhibit hPIV3 minigenome replication. In contrast, the C protein of hPIV3 inhibited minigenome replication of hPIV3, NiV and MV. Although there is very limited amino acid sequence similarity between the C, V and W proteins within the paramyxoviruses, the heterotypic inhibition of replication suggests that these proteins may share functional properties. INTRODUCTIONNipah virus (NiV) is a recently emergent, highly pathogenic, zoonotic paramyxovirus. NiV was first identified in Malaysia in 1998 during an outbreak of neurological and respiratory disease in swine, which resulted in severe febrile encephalitis in humans who had contact with infected pigs (Chua et al., 2000). NiV has been associated with subsequent outbreaks of fatal, febrile encephalitis in Bangladesh and India between (Hsu et al., 2004Luby et al., 2006). Molecular characterization of NiV revealed that it was related closely to Hendra virus, another zoonotic paramyxovirus, which had emerged in Australia in 1994 (Chua et al., 2000;Harcourt et al., 2000Harcourt et al., , 2001. These two viruses constitute the recently recognized genus Henipavirus (Mayo, 2002).The genome of NiV is 18 246 nt in length and contains six transcription units encoding six viral structural proteins (39-N-P-M-F-G-L-59) and three predicted non-structural proteins, C, V and W . As in other paramyxoviruses, the C protein of NiV is expressed from an alternative open reading frame (ORF) within the phosphoprotein (P) gene, whereas the V and W proteins are expressed by RNA editing (Lamb & Kolakofsky, 2001). At a unique, highly conserved RNA-editing site in the P gene, the polymerase protein (L) inserts a single, nontemplated G residue that results in a frame shift and the expression of the V protein. Insertion of two nontemplated G residues results in expression of the W protein . Whilst the C proteins of NiV and of other paramyxoviruses are unique and share no sequence similarity with the P protein (Lamb & Kolakofsky, 2001), the V and W proteins share an amino-terminal 407 aa domain with P and each possesses a unique carboxyl-terminal domain consisting of 52 aa for V and 47 aa for W . The sequences of the P proteins of paramyxoviruses a...

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“…RPV that does not express the C protein, on the other hand, is clearly impaired for growth in cell culture, and its mRNA transcription is reduced (3). The RPV V and C proteins were found to interact with the L protein (54). Recently, the negative modulatory activity of V proteins encoded by PIV5 and MeV has been reproduced in transient minireplicon expression systems (32,62).…”

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confidence: 99%

Human Parainfluenza Virus Type 2 V Protein Inhibits Genome Replication by Binding to the L Protein: Possible Role in Promoting Viral Fitness

Nishio

Ohtsuka

Tsurudome

et al. 2008

J Virol

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The human parainfluenza virus type 2 (hPIV2) V protein plays important roles in inhibiting the host interferon response and promoting virus growth, but its role in hPIV2 replication and transcription is not clear. A green fluorescent protein (GFP)-expressing a negative-sense minigenomic construct of hPIV2 has been established by standard technology, with helper plasmids expressing the nucleocapsid protein (NP), phosphoprotein (P), and large RNA polymerase (L) protein, to examine the role of V protein. We found that the simultaneous expression of wild-type V protein in the minigenome system inhibited GFP expression, at least in part, by inhibiting minigenome replication. In contrast, expression of C terminally truncated or mutant hPIV2 V proteins had no effect. Moreover, the V protein of simian virus 41, the rubulavirus most closely related virus to hPIV2, also inhibited GFP expression, whereas that of PIV5, a more distantly related rubulavirus, did not. Using these other rubulavirus V proteins, as well as various mutant hPIV2 V proteins, we found that the ability of V protein to inhibit GFP expression correlated with its ability to bind to L protein via its C-terminal V protein-specific region, but there was no correlation with NP binding. A possible role for this inhibition of genome replication in promoting viral fitness is discussed.Human parainfluenza virus type 2 (hPIV2) is a member of the Rubulavirus genus of the family Paramyxoviridae. This family includes many well-known human and animal pathogens, such as Sendai virus (SeV), hPIV types 1 to 4, simian virus 41 (SV41), parainfluenza virus type 5 (PIV5; formerly known as SV5), mumps virus, Newcastle disease virus, measles virus (MeV), and respiratory syncytial virus, as well as important emerging viruses such as Hendra and Nipah viruses. The negative-stranded RNA genome of hPIV2 is 15,654 nucleotides long and encodes seven viral proteins from six genes (30). The nucleocapsid protein (NP), phosphoprotein (P), and large RNA polymerase (L) protein are important for transcription and replication of the viral RNA genome. All viruses of the Paramyxoviridae (with the notable exception of hPIV1) contain an mRNA-editing site at which G residues are inserted into the P gene mRNA in a programmed manner during its synthesis. In respiroviruses and morbilliviruses, the P mRNA is a faithful copy of the genome RNA, and the V mRNA results from the insertion of one additional pseudotemplated G nucleotide. In only rubulaviruses, it is the V mRNA that is a faithful transcript of the V/P gene, whereas the P mRNA is synthesized through a cotranscriptional insertion of two pseudotemplated G residues. Thus, the N-terminal 164 amino acids (aa) of the V and P proteins are common, while their C termini are unique (43). Since insertion of the G residues in hPIV2 occurs ca. 50% of the time, roughly equal amounts of V and P mRNAs are produced. The C termini of the V proteins contain seven invariant cysteines that bind two atoms of zinc and is ca. 50% identical in sequence among all par...

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Rinderpest Virus C and V Proteins Interact with the Major (L) Component of the Viral Polymerase

Cited by 39 publications

References 80 publications

Rinderpest Virus Blocks Type I and Type II Interferon Action: Role of Structural and Nonstructural Proteins

Rinderpest Virus Blocks Type I and Type II Interferon Action: Role of Structural and Nonstructural Proteins

The C, V and W proteins of Nipah virus inhibit minigenome replication

Human Parainfluenza Virus Type 2 V Protein Inhibits Genome Replication by Binding to the L Protein: Possible Role in Promoting Viral Fitness

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