Genomic Organization of the Structural Proteins of Borna Disease Virus Revealed by a cDNA Clone Encoding the 38-kDa Protein

Pyper, J. M.; Richt, Jürgen A.; Brown, Lesley R.; Rott, R.; Narayan, Opendra; Clements, Janice E.

doi:10.1006/viro.1993.1364

Cited by 39 publications

(41 citation statements)

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“…Restriction fragments representing the five ORFs were used as probes for hybridization to poly(A)+ RNA isolated from acutely infected rat brain by FastTrack (Fig. 4a and b CoC--n- (27). Transcriptional readthrough was also found the more 5' probes (Fig.…”

Section: Resultsmentioning

confidence: 99%

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Genomic organization of Borna disease virus.

Briese

Schneemann

Lewis

et al. 1994

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

282

327

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Borna disease virus is a neurotropic negativestrand RNA virus that infects a wide range of vertebrate hosts, causing disturbances in movement and behavior. We have cloned and sequenced the 8910-nucleotide viral genome by using RNA from Borna disease virus particles. The viral genome has complementary 3' and 5' termini and contains antisense information for five open reading frames. Homology to Filoviridae, Paramyxoviridae, and Rhabdoviridae is found in both cistronic and extracistronic regions. Northern analysis indicates that the virus transcribes mono-and polycistronic RNAs and uses terminatlon/polyadenylylation signals reminiscent ofthose observed in other negative-strand RNA viruses. Borna disease virus is likely to represent a previously unrecognized genus, bornaviruses, or family, Bornaviridae, within the order Mononegavirales.

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Section: Resultsmentioning

confidence: 99%

“…Due to a more favorable translation initiation context (30), it is likely that the second AUG codon, 39 nt inside the ORF, is used to express a 357-aa protein of 39.5 kDa (p40) (27). Twenty-six nucleotides downstream of the stop codon is a polyadenylylation signal (19) (T2, Fig.…”

Section: Discussionmentioning

confidence: 99%

Genomic organization of Borna disease virus.

Briese

Schneemann

Lewis

et al. 1994

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

282

327

View full text Add to dashboard Cite

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“…BDV contains at least six different proteins. Of these proteins, the nucleoprotein (N) and phosphoprotein (P) are major products of BDV and are abundantly expressed in infected cultured cells and animal brains (17,24,35,43,44). In addition, a small open reading frame (ORF), X, which overlaps the P ORF, encodes another major protein (X) of BDV (47).…”

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confidence: 99%

Modulation of Borna Disease Virus Phosphoprotein Nuclear Localization by the Viral Protein X Encoded in the Overlapping Open Reading Frame

Kobayashi

Zhang

Lee

et al. 2003

J Virol

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Borna disease virus (BDV) is a nonsegmented, negative-strand RNA virus that belongs to the Mononegavirales order. Unlike other animal viruses in this order, BDV replicates and transcribes in the nucleus of infected cells. Therefore, regulation of the intracellular movement of virus components must be critical for accomplishing the BDV life cycle in mammalian cells. Previous studies have demonstrated that BDV proteins are prone to accumulate in the nucleus of cells transiently transfected with each expression plasmid of the viral proteins. In BDV infection, however, cytoplasmic distribution of the viral proteins is frequently found in cultured cells and animal brains. In this study, to understand the modulation of subcellular localization of BDV proteins, we investigated the intracellular localization of the viral phosphoprotein (P). Transienttransfection analysis with a cDNA clone corresponding to a bicistronic transcript that expresses both viral X and P revealed that P efficiently localizes in the cytoplasm only when BDV X is expressed in the cells. Furthermore, our analysis revealed that the direct binding between X and P is necessary for the cytoplasmic localization of the P. Interestingly, we showed that X is not detectably expressed in the BDV-infected cells in which P is predominantly found in the nucleus, with little or no signal in the cytoplasm. These observations suggested that BDV P can modulate their subcellular localization through binding to X and that BDV may regulate the expression ratio of each viral product in infected cells to control the intracellular movement of the viral protein complexes. The results presented here provide a new insight into the regulation of the intracellular movement of viral proteins of a unique, nonsegmented, negative-strand RNA virus.

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“…Molecular biological analysis has indicated that the BDV antigenome consists of at least six open reading frames (ORFs). The ORFs encode nucleoprotein (N), phosphoprotein (P), matrix protein, envelope protein, and a predicted RNA-dependent RNA polymerase in the 5Ј-to-3Ј order (12,17,18,23,35,38,43,44,46). In addition, a small ORF X, which overlaps the P ORF, was identified to encode a novel protein X of unknown function (49).…”

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Borna Disease Virus Nucleoprotein Requires both Nuclear Localization and Export Activities for Viral Nucleocytoplasmic Shuttling

Kobayashi

Kamitani

Zhang

et al. 2001

J Virol

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Nuclear transport of viral nucleic acids is crucial to the life cycle of many viruses. Borna disease virus (BDV)belongs to the order Mononegavirales and replicates its RNA genome in the nucleus. Previous studies have suggested that BDV nucleoprotein (N) and phosphoprotein (P) have important functions in the nuclear import of the viral ribonucleoprotein (RNP) complexes via their nuclear targeting activity. Here, we showed that BDV N has cytoplasmic localization activity, which is mediated by a nuclear export signal (NES) within the sequence. Our analysis using deletion and substitution mutants of N revealed that NES of BDV N consists of a canonical leucine-rich motif and that the nuclear export activity of the protein is mediated through the chromosome region maintenance protein-dependent pathway. Interspecies heterokaryon assay indicated that BDV N shuttles between the nucleus and cytoplasm as a nucleocytoplasmic shuttling protein. Furthermore, interestingly, the NES region overlaps a binding site to the BDV P protein, and nuclear export of a 38-kDa form of BDV N is prevented by coexpression of P. These results suggested that BDV N has two contrary activities, nuclear localization and export activity, and plays a critical role in the nucleocytoplasmic transport of BDV RNP by interaction with other viral proteins.Many viruses, including influenza viruses, herpesviruses, and retroviruses, replicate in the nucleus. Therefore, nuclear import and export of the viral genome are critical to the life cycle of viruses in mammalian cells. It has been reported that these virus employ mechanisms by which the viral nucleic acids enter and leave the nucleus in association with their replication stages (51). In human immunodeficiency virus type 1 (HIV-1), viral proteins including integrase, matrix (MA), and Vpr promote localization of the viral preintegration complex (PIC) to the nucleus following the entry of virus into a cell (4,10,33,45). The MA protein harbors nuclear export activity, in addition to nuclear localization activity, to direct the viral RNAs to the cytoplasm (8). Rev proteins of HIV-1 also have both these nuclear transport activities to transport unspliced or single spliced viral transcripts (32). On the other hand, the nucleocapsid protein (NP) and the nonstructural proteins (NS2 and NEP) of influenza A virus are required for nuclear import and export of the viral ribonucleoprotein (RNP) complex, respectively (9, 28-31, 47). Furthermore, matrix protein (M1) of the influenza virus also plays an essential role in RNP nuclear export in combination with other viral proteins (51). Studies of these nuclear transport proteins revealed that they contain specific signals that mediate nuclear transport, called the nuclear localization signal (NLS) and the nuclear export signal (NES), which function independently of the surrounding sequences (27, 51). NLS-or NES-containing proteins can directly or indirectly bind to the viral nucleic acids and travel between the cytoplasm and nucleus through the nuclear pore complex (13...

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Genomic Organization of the Structural Proteins of Borna Disease Virus Revealed by a cDNA Clone Encoding the 38-kDa Protein

Cited by 39 publications

References 0 publications

Genomic organization of Borna disease virus.

Genomic organization of Borna disease virus.

Modulation of Borna Disease Virus Phosphoprotein Nuclear Localization by the Viral Protein X Encoded in the Overlapping Open Reading Frame

Borna Disease Virus Nucleoprotein Requires both Nuclear Localization and Export Activities for Viral Nucleocytoplasmic Shuttling

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