The Rotavirus RNA-Binding Protein NS35 (NSP2) Forms 10S Multimers and Interacts with the Viral RNA Polymerase

Kattoura, Maha D.; Chen, Xia; Patton, John T.

doi:10.1006/viro.1994.1402

Cited by 72 publications

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“…NSP2 is a rotaviral non-structural protein which has been previously found to interact also with the viral polymerase and to form homomultimers (Kattoura et al, 1994). NSP2 binds to viral ssRNAs and can be cross-linked in vivo to the 11 dsRNA genomic segments.…”

Section: Discussionmentioning

confidence: 99%

“…NSP2 has been reported to interact with VP1 (Kattoura et al, 1994). Recently, using a monoclonal anti-NSP2 antibody, a viral RNA-protein complex with replicase activity was recovered (Aponte et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

“…Although several reports have described the characterization of rotavirus replication intermediates (Gallegos & Patton, 1989 ;Patton & Gallegos, 1988), molecular details of the replication mechanism remain unclear. Partially purified intermediate complexes (or sub-viral particles) obtained from SA11-infected cells were able to catalyse run-off synthesis of endogenous dsRNAs (Patton, 1986), as well as complete replication of exogenously added viral ss (j)-RNAs (Chen et al, 1994 ;Wentz et al, 1996 ;Patton et al, 1996 ;E. Fabbretti & O. R. Burrone, unpublished).…”

Section: Introductionmentioning

confidence: 99%

“…Strains expressing temperature-sensitive mutants of this protein lose the ability to synthesize dsRNA and show a significant reduction in the synthesis of ssRNA (Chen et al, 1990). It has been shown that NSP2 is able to assemble in multimers and interact with the viral polymerase, VP1 (Kattoura et al, 1994). NSP5 is encoded in the longer ORF of genomic segment 11.…”

Section: Introductionmentioning

confidence: 99%

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Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2.

Afrikanova

Fabbretti

Miozzo

et al. 1998

Journal of General Virology

129

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We have previously shown that a number of isoforms of the non-structural rotavirus protein NSP5 are found in virus-infected cells. These isoforms differ in their level of phosphorylation which, at least in part, appears to occur through autophosphorylation. NSP5 co-localizes with another non-structural protein, NSP2, in the viroplasms of infected cells where virus replication takes place. We now show that NSP5 can be chemically cross-linked in living cells with the viral polymerase VP1 and NSP2. Interaction of NSP5 with NSP2 was also demonstrated by coimmunoprecipitation of NSP2 and NSP5 from extracts of UV-treated rotavirus-infected cells. In

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2.

Afrikanova

Fabbretti

Miozzo

et al. 1998

Journal of General Virology

129

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“…Both NP2 and NSP5 accumulate in viroplasms, and the expression of these proteins together, but not separately, generates viroplasm-like structures in uninfected cells (12). NSP2 has strong sequence-independent affinity for single-stranded RNA (ssRNA) (20), interacts with the viral RNA polymerase (19), and self-assembles into stable octamers (44). The NSP2 octamers have Mg 2ϩ -dependent NTPase activity (47) and Mg 2ϩ -independent helix-destabilizing activity (46).…”

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confidence: 99%

RNA-Binding Activity of the Rotavirus Phosphoprotein NSP5 Includes Affinity for Double-Stranded RNA

Vende

Taraporewala

Patton

2002

J Virol

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Phosphoprotein NSP5 is a component of replication intermediates that catalyze the synthesis of the segmented double-stranded RNA (dsRNA) rotavirus genome. To study the role of the protein in viral replication, His-tagged NSP5 was expressed in bacteria and purified by affinity chromatography. In vitro phosphorylation assays showed that NSP5 alone contains minimal autokinase activity but undergoes hyperphosphorylation when combined with the NTPase and helix-destabilizing protein NSP2. Hence, NSP2 mediates the hyperphosphorylation of NSP5 in the absence of other viral or cellular proteins. RNA-binding assays demonstrated that NSP5 has unique nonspecific RNA-binding activity, recognizing single-stranded RNA and dsRNA with similar affinities. The possible functions of the RNA-binding activities of NSP5 are to cooperate with NSP2 in the destabilization of RNA secondary structures and in the packaging of RNA and/or to prevent the interferoninduced dsRNA-dependent activation of the protein kinase PKR.

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Iron–Sulfur Clusters in Viral Diseases

Raza

Karges

2023

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Iron–sulfur [Fe–S] clusters are among the oldest cofactors known on earth. These compounds are structurally and functionally highly versatile and therefore used in various biological processes including biochemical catalysis, electron transfer reactions, sulfur donation, as well as sensing. To date, the presence of functioning [Fe–S] clusters has been verified in all types of living organisms including bacteria, archaea, and eukaryotes. Studies have shown that the biological activity of the [Fe–S] cluster is mainly attributed to its highly accessible and reversible redox activity, which can range over several oxidation and spin states. Over the last years, [Fe–S] clusters have been identified as a key component in various viral diseases including but not limited to polyomaviruses, rotaviruses, hepatitis b virus, and coronaviruses. Within this article, the potential role of [Fe–S] clusters in viral diseases is critically reviewed.

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The Rotavirus RNA-Binding Protein NS35 (NSP2) Forms 10S Multimers and Interacts with the Viral RNA Polymerase

Cited by 72 publications

References 0 publications

Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2.

Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2.

RNA-Binding Activity of the Rotavirus Phosphoprotein NSP5 Includes Affinity for Double-Stranded RNA

Iron–Sulfur Clusters in Viral Diseases

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