Identification of a Major Non-structural Protein in the Nuclei of Rift Valley Fever Virus-infected Cells

Struthers, J. K.; Swanepoel, Robert

doi:10.1099/0022-1317-60-2-381

Cited by 57 publications

(37 citation statements)

References 4 publications

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“…4D). Nuclear filaments are consistent with the expected localization of authentic NSs in RVFV-infected cells (55)(56)(57). PABP1 accumulated in the nuclei of several but not all cells expressing NSs.…”

Section: Pabp1 Relocalizes To Nuclear Speckles During Rvfv Infectionsupporting

confidence: 83%

Nuclear Relocalization of Polyadenylate Binding Protein during Rift Valley Fever Virus Infection Involves Expression of the NSs Gene

Copeland

Altamura

Deusen

et al. 2013

J Virol

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Rift Valley fever virus (RVFV), an ambisense member of the family Bunyaviridae, genus Phlebovirus, is the causative agent of Rift Valley fever, an important zoonotic infection in Africa and the Middle East. Phlebovirus proteins are translated from virally transcribed mRNAs that, like host mRNA, are capped but, unlike host mRNAs, are not polyadenylated. Here, we investigated the role of PABP1 during RVFV infection of HeLa cells. Immunofluorescence studies of infected cells demonstrated a gross relocalization of PABP1 to the nucleus late in infection. Immunofluorescence microscopy studies of nuclear proteins revealed costaining between PABP1 and markers of nuclear speckles. PABP1 relocalization was sharply decreased in cells infected with a strain of RVFV lacking the gene encoding the RVFV nonstructural protein S (NSs). To determine whether PABP1 was required for RVFV infection, we measured the production of nucleocapsid protein (N) in cells transfected with small interfering RNAs (siRNAs) targeting PABP1. We found that the overall percentage of RVFV N-positive cells was not changed by siRNA treatment, indicating that PABP1 was not required for RVFV infection. However, when we analyzed populations of cells producing high versus low levels of PABP1, we found that the percentage of RVFV N-positive cells was decreased in cell populations producing physiologic levels of PABP1 and increased in cells with reduced levels of PABP1. Together, these results suggest that production of the NSs protein during RVFV infection leads to sequestration of PABP1 in the nuclear speckles, creating a state within the cell that favors viral protein production.

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Section: Pabp1 Relocalizes To Nuclear Speckles During Rvfv Infectionsupporting

confidence: 83%

Nuclear Relocalization of Polyadenylate Binding Protein during Rift Valley Fever Virus Infection Involves Expression of the NSs Gene

Copeland

Altamura

Deusen

et al. 2013

J Virol

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“…Noteworthy is that the function of the protein in the virus life cycle has not yet been determined and that its localization in infected cells, as well as its presence in viral particles, varies depending on the virus. With the exception of the NS S protein from RVF virus, which has been reported to form filaments in the nuclei of infected cells (Struthers & Swanepoel, 1982 ;Struthers et al, 1984), the NS S protein of the phleboviruses studied was detected in the cytoplasm. In the case of Uukuniemi virus, Simons et al (1992) demonstrated that the protein was associated with the 40S ribosomal subunit and not detected in mature particles.…”

Section: Phylogenetic Analysis Of the Rvf Virus Ns S Genesmentioning

confidence: 87%

Variability of the NS(S) protein among Rift Valley fever virus isolates.

Sall

Zanotto

Zeller

et al. 1997

Journal of General Virology

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Eighteen strains of Rift Valley fever (RVF) virus collected over a period of 38 years and isolated from diverse localities in Africa and from various hosts (human, animal and arthropod) were investigated by RT-PCR followed by sequencing of the NS S protein coding region. This region was chosen to analyse variability because, in contrast to the N protein, the NS S protein differs in various phleboviruses and there exists an RVF virus (clone 13) in which 70 % of the NS S ORF is deleted, suggesting that this sequence is under a weak selective pressure. Sequence data indicated that percentage di-

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“…There are 13 amino acid differences between the PTV-A and PTV-B strains which would be ideal targets for site-directed mutagenesis and mapping of this protein's IFNantagonistic ability. There is little amino acid sequence identity (27 common residues of an alignment of 250) between the RVFV and PTV NSs proteins, and it is currently unknown if the PTV NSs protein localizes to the nucleus (7,35,41).…”

Section: Discussionmentioning

confidence: 99%

The S Segment of Punta Toro Virus ( Bunyaviridae , Phlebovirus ) Is a Major Determinant of Lethality in the Syrian Hamster and Codes for a Type I Interferon Antagonist

Perrone¹,

Narayanan

Worthy

et al. 2007

J Virol

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Identification of a Major Non-structural Protein in the Nuclei of Rift Valley Fever Virus-infected Cells

Cited by 57 publications

References 4 publications

Nuclear Relocalization of Polyadenylate Binding Protein during Rift Valley Fever Virus Infection Involves Expression of the NSs Gene

Nuclear Relocalization of Polyadenylate Binding Protein during Rift Valley Fever Virus Infection Involves Expression of the NSs Gene

Variability of the NS(S) protein among Rift Valley fever virus isolates.

The S Segment of Punta Toro Virus ( Bunyaviridae , Phlebovirus ) Is a Major Determinant of Lethality in the Syrian Hamster and Codes for a Type I Interferon Antagonist

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