Rift Valley Fever Virus Nonstructural Protein NSs Promotes Viral RNA Replication and Transcription in a Minigenome System

Ikegami, Tetsuro; Peters, C. J.; Makino, Shinji

doi:10.1128/jvi.79.9.5606-5615.2005

Cited by 97 publications

(115 citation statements)

References 30 publications

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“…The S (small) segment encodes the N protein and a second nonstructural protein, NSs. NSs, a viral virulence factor, is a transcriptional repressor critical to the down-regulation of the host interferon response (7)(8)(9)(10)(11)(12)(13)(14)(15)(16).…”

Section: Rift Valley Fever Virus (Rvfv)mentioning

confidence: 99%

Curcumin Inhibits Rift Valley Fever Virus Replication in Human Cells

Narayanan

Kehn-Hall

Senina

et al. 2012

Journal of Biological Chemistry

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Background: Rift Valley fever virus is a single-stranded RNA virus that causes disease in humans and livestock. Results: Rift Valley fever virus infection activates the host NFB signaling cascade. Conclusion: NFB inhibitors, particularly curcumin, down-regulate virus in both in vitro and in vivo models. Significance: Novel versions of host components resulting from an infection make them ideal therapeutic targets.

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Section: Rift Valley Fever Virus (Rvfv)mentioning

confidence: 99%

Curcumin Inhibits Rift Valley Fever Virus Replication in Human Cells

Narayanan

Kehn-Hall

Senina

et al. 2012

Journal of Biological Chemistry

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“…2A). Western blot analysis using anti-myc antibody and anti-NSs antibody (27) confirmed expression of nsp1 protein and NSs protein, respectively (data not shown). Western blot analysis of SeV N protein (Fig.…”

Section: Nsp1 Protein Suppresses Ifn-␤ Mrna Accumulation Without Inhimentioning

confidence: 99%

“…At 48 h after transfection, cell extracts were prepared. Western blot analysis using anti-myc antibody, antiNSs antibody (27), and anti-3a antibody (29) confirmed expression of nsp1, NSs, and 3a protein, respectively (data not shown). NSs expression resulted in low ␤-gal activity most probably because of the NSs-mediated general suppression of mRNA synthesis (22), whereas expression of SCoV 3a protein modestly suppressed ␤-gal activity.…”

Section: Nsp1 Protein Suppresses Ifn-␤ Mrna Accumulation Without Inhimentioning

confidence: 99%

“…The RT-PCR product corresponding to SCoV nsp1 ORF was cloned into pCAGGS-MCS, resulting in pCAGGS-nsp1, in which myc-tag was added to the C terminus of the nsp1 ORF. The cDNA encoding the entire wild-type RVFV NSs ORF region (27) was cloned into pCAGGS, yielding pCAGGS-NSs. The construction of pCAGGS-3a, expressing a SCoV accessory protein 3a, was described (28).…”

Section: Methodsmentioning

confidence: 99%

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Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression by promoting host mRNA degradation

Kamitani

Narayanan

Huang

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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412

498

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“…The characteristic feature of the hantaviral genome is the partially complementary sequence at the 5Ј and 3Ј termini of each of the three genome segments that undergo base pairing and form panhandle structures (4 -6). N is a multifunctional protein playing a vital role in multiple processes of virus replication cycle and has been found to undergo trimerization both in vivo and in vitro (7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19). During encapsidation, the three viral RNA (vRNA) molecules are specifically recognized by N inside the host cell and targeted for packaging.…”

mentioning

confidence: 99%

Hantavirus Nucleocapsid Protein Has Distinct m7G Cap- and RNA-binding Sites

Mir

Sheema

Haseeb

et al. 2010

Journal of Biological Chemistry

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Hantaviruses, members of the Bunyaviridae family, are emerging category A pathogens that carry three negative stranded RNA molecules as their genome. Hantavirus nucleocapsid protein (N) is encoded by the smallest S segment genomic RNA (viral RNA). N specifically binds mRNA caps and requires four nucleotides adjacent to the cap for high affinity binding. We show that the N peptide has distinct cap-and RNA-binding sites that independently interact with mRNA cap and viral genomic RNA, respectively. In addition, N can simultaneously bind with both mRNA cap and vRNA. N undergoes distinct conformational changes after binding with either mRNA cap or vRNA or both mRNA cap and vRNA simultaneously. Hantavirus RNA-dependent RNA polymerase (RdRp) uses a capped RNA primer for transcription initiation. The capped RNA primer is generated from host cell mRNA by the cap-snatching mechanism and is supposed to anneal with the 3 terminus of vRNA template during transcription initiation by single G-C base pairing. We show that the capped RNA primer binds at the cap-binding site and induces a conformational change in N. The conformationally altered N with a capped primer loaded at the cap-binding site specifically binds the conserved 3 nine nucleotides of vRNA and assists the bound primer to anneal at the 3 terminus. We suggest that the cap-binding site of N, in conjunction with RdRp, plays a key role during the transcription and replication initiation of vRNA genome.Hantaviruses cause two types of serious human illnesses when transmitted to humans from rodent hosts: hemorrhagic fever with renal syndrome and hantavirus cardiopulmonary syndrome (1, 2). The spherical hantavirus particles harbor three negative sense genomic RNA segments (S, L, and M segments) within a lipid bilayer (3). The mRNAs derived from S, L, and M segments encode viral nucleocapsid protein (N), viral RNA-dependent RNA polymerase (RdRp), 2 and glycoproteins (G1 and G2), respectively. The characteristic feature of the hantaviral genome is the partially complementary sequence at the 5Ј and 3Ј termini of each of the three genome segments that undergo base pairing and form panhandle structures (4 -6). N is a multifunctional protein playing a vital role in multiple processes of virus replication cycle and has been found to undergo trimerization both in vivo and in vitro (7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19). During encapsidation, the three viral RNA (vRNA) molecules are specifically recognized by N inside the host cell and targeted for packaging. Multiple in vitro studies have shown that N preferentially binds vRNA compared with complementary RNA (cRNA) or nonviral RNA (13, 20 -25). It has been proposed that the specific binding of N with either the panhandle or the sequence at the 5Ј terminus alone selectively facilitates the encapsidation of vRNA to generate three nucleocapsids that are packaged into infectious virions (25, 26). The RNA-binding domain of Hantaan virus N protein has been mapped to the central conserved region corresponding to amino acids f...

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Rift Valley Fever Virus Nonstructural Protein NSs Promotes Viral RNA Replication and Transcription in a Minigenome System

Abstract: Rift Valley fever virus (RVFV), which belongs to the genus Phlebovirus, family Bunyaviridae, has a tripartite negative-strand genome (S, M, and L segments) and is an important

Cited by 97 publications

References 30 publications

Curcumin Inhibits Rift Valley Fever Virus Replication in Human Cells

Curcumin Inhibits Rift Valley Fever Virus Replication in Human Cells

Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression by promoting host mRNA degradation

Hantavirus Nucleocapsid Protein Has Distinct m7G Cap- and RNA-binding Sites

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