Rescue of Recombinant Marburg Virus from cDNA Is Dependent on Nucleocapsid Protein VP30

Enterlein, Sven; Volchkov, Viktor E.; Weik, Michael; Kolesnikova, Larissa; Volchkova, Valentina A.; Klenk, Hans‐Dieter; Mühlberger, Elke

doi:10.1128/jvi.80.2.1038-1043.2006

Cited by 72 publications

(72 citation statements)

References 30 publications

(35 reference statements)

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“…In addition, RNA interference targeting MARV VP30 led to the down-regulation of the intracellular levels of all other viral proteins in infected cells, thereby suggesting that VP30 plays an essential role in transcription/replication [63]. However, in contrast to EBOV, a MARV VP30 mutant containing a destroyed zinc-binding motif was able to mediate the rescue of a full-length MARV clone [62]. Thus, it appears that MARV VP30 is essential for the viral life cycle but probably not involved in transcription activation.…”

Section: Filovirus Transcriptionmentioning

confidence: 94%

“…Whether MARV VP30 is involved in transcription activation remains elusive. Although transcription took place independently of VP30 in a reconstituted MARV minigenome system, a full-length MARV clone could only be recovered when MARV VP30 was added as a helper plasmid [62]. In addition, RNA interference targeting MARV VP30 led to the down-regulation of the intracellular levels of all other viral proteins in infected cells, thereby suggesting that VP30 plays an essential role in transcription/replication [63].…”

Section: Filovirus Transcriptionmentioning

confidence: 99%

“…• Based on the minigenome system, rescue systems have been established for MARV and EBOV, allowing the recovery of complete recombinant viruses entirely from cDNA ( Figure 3) [29,55,62,73].…”

Section: • For a Long Time Research On Marburg (Marv) And Ebola Virumentioning

confidence: 99%

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Filovirus Replication and Transcription

2007

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The highly pathogenic filoviruses, Marburg and Ebola virus, belong to the nonsegmented negative-sense RNA viruses of the order Mononegavirales. The mode of replication and transcription is similar for these viruses. On one hand, the negative-sense RNA genome serves as a template for replication, to generate progeny genomes, and, on the other hand, for transcription, to produce mRNAs. Despite the similarities in the replication/transcription strategy, filoviruses have evolved structural and functional properties that are unique among the nonsegmented negativesense RNA viruses. Moreover, there are also striking differences in the replication and transcription mechanisms of Marburg and Ebola virus. This includes nucleocapsid formation, the structure of the genomic replication promoter, the protein requirement for transcription and the use of mRNA editing. In this article, the current knowledge of the replication and transcription strategy of Marburg and Ebola virus is reviewed, with focus on the observed differences.

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Section: Filovirus Transcriptionmentioning

confidence: 94%

Section: Filovirus Transcriptionmentioning

confidence: 99%

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Filovirus Replication and Transcription

2007

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“…This has been demonstrated with systems analogous to the minigenome system described above (28)(29)(30). The minimal set of filoviral proteins required for transcription and replication for MARV are NP, VP35, and L, although recovery of recombinant MARVs from cDNA also required expression of VP30 (9). Transcription of EBOV subgenomic replicon RNAs requires NP, VP35, VP30, and L; however, the replication reaction can proceed in the absence of VP30 (5,30).…”

Section: Discussionmentioning

confidence: 99%

Basic Residues within the Ebolavirus VP35 Protein Are Required for Its Viral Polymerase Cofactor Function

Prins

Binning

Shabman

et al. 2010

J Virol

139

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The ebolavirus (EBOV) VP35 protein binds to double-stranded RNA (dsRNA), inhibits host alpha/beta interferon (IFN-␣/␤) production, and is an essential component of the viral polymerase complex. Structural studies of the VP35 C-terminal IFN inhibitory domain (IID) identified specific structural features, including a central basic patch and a hydrophobic pocket, that are important for dsRNA binding and IFN inhibition. Several other conserved basic residues bordering the central basic patch and a separate cluster of basic residues, called the first basic patch, were also identified. Functional analysis of alanine substitution mutants indicates that basic residues outside the central basic patch are not required for dsRNA binding or for IFN inhibition. However, minigenome assays, which assess viral RNA polymerase complex function, identified these other basic residues to be critical for viral RNA synthesis. Of these, a subset located within the first basic patch is important for VP35-nucleoprotein (NP) interaction, as evidenced by the inability of alanine substitution mutants to coimmunoprecipitate with NP. Therefore, first basic patch residues are likely critical for replication complex formation through interactions with NP. Coimmunoprecipitation studies further demonstrate that the VP35 IID is sufficient to interact with NP and that dsRNA can modulate VP35 IID interactions with NP. Other basic residue mutations that disrupt the VP35 polymerase cofactor function do not affect interaction with NP or with the amino terminus of the viral polymerase. Collectively, these results highlight the importance of conserved basic residues from the EBOV VP35 C-terminal IID and validate the VP35 IID as a potential therapeutic target.

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“…VP30 appears unique to the filoviruses and is essential for rescuing recombinant ebolavirus (Enterlein et al, 2006;Theriault et al, 2004). VP30 allows the polymerase to read beyond a cis-RNA element in the NP mRNA 5 0 untranslated region (Weik et al, 2002) and to re-initiate transcription at gene junctions (Martínez et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Structure of theReston ebolavirusVP30 C-terminal domain

Clifton¹,

Kirchdoerfer

Atkins³

et al. 2014

Acta Cryst Sect F

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PDB reference: Reston ebolavirus VP30 C-terminal domain, 3v7oThe ebolaviruses can cause severe hemorrhagic fever. Essential to the ebolavirus life cycle is the protein VP30, which serves as a transcriptional cofactor. Here, the crystal structure of the C-terminal, NP-binding domain of VP30 from Reston ebolavirus is presented. Reston VP30 and Ebola VP30 both form homodimers, but the dimeric interfaces are rotated relative to each other, suggesting subtle inherent differences or flexibility in the dimeric interface.

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Rescue of Recombinant Marburg Virus from cDNA Is Dependent on Nucleocapsid Protein VP30

Cited by 72 publications

References 30 publications

Filovirus Replication and Transcription

Filovirus Replication and Transcription

Basic Residues within the Ebolavirus VP35 Protein Are Required for Its Viral Polymerase Cofactor Function

Structure of theReston ebolavirusVP30 C-terminal domain

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