Antigenic relationship and further characterization of two major Borna disease virus-specific proteins

Thiedemann, Norbert; Presek, Peter; Rott, R.; Stitz, Lothar

doi:10.1099/0022-1317-73-5-1057

Cited by 62 publications

(55 citation statements)

References 33 publications

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“…The absence of carbohydrate side-chains is in accordance with the intranuclear localization of the p10 protein in persistently BDV-infected MDCK cells ; in immuno-fluorescence experiments the distribution of p10 in the cell nucleus was similar to that demonstrated previously for the BDV p24 and p38 proteins (Haas et al, 1986 ;Thiedemann et al, 1992). Double staining with anti-p10 and anti-p38 antibodies showed that p10 accumulated at the same sites in the nucleus of BDVinfected MDCK cells as p38.…”

Section: Cegesupporting

confidence: 56%

“…The p24 protein appears to be a different, unrelated protein. Neither the p38 nor the p24 proteins are glycosylated and both are soluble proteins ; the p24 protein is phosphorylated (Thiedemann et al, 1992). The gp18 protein is a membrane-associated glycoprotein with an unusual N-linked glycosylation pattern (Kliche et al, 1994), which apparently contains epitopes important for virus neutralization (Hatalski et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Detection of a novel Borna disease virus-encoded 10 kDa protein in infected cells and tissues.

Wehner¹,

Ruppert²,

Herden³

et al. 1997

Journal of General Virology

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Section: Cegesupporting

confidence: 56%

Section: Introductionmentioning

confidence: 99%

Detection of a novel Borna disease virus-encoded 10 kDa protein in infected cells and tissues.

Wehner¹,

Ruppert²,

Herden³

et al. 1997

Journal of General Virology

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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).…”

mentioning

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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“…Encephalitic infiltrates were scored on an arbitrary scale ranging from 0 to 3 based on the number of infiltrates per section and the number of cell layers in each infiltrate (score 1, up to 5 small infiltrates per section; score 2, more than 5 small infiltrates per section or more than 3 infiltrates with multiple layers; score 3, more than 10 small infiltrates per section or more than 5 infiltrates with multiple layers). Immunohistochemistry was carried out on cryostat sections for the presence of BDVspecific antigen, using an anti-nucleoprotein-specific monoclonal antibody (38/ 17C1) (36).…”

Section: Viruses and Infection (I) Bdv-brmentioning

confidence: 99%

High-Dose Borna Disease Virus Infection Induces a Nucleoprotein-Specific Cytotoxic T-Lymphocyte Response and Prevention of Immunopathology

Furrer¹,

Bilzer

Stitz³

et al. 2001

J Virol

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؉ T cells could be demonstrated in the brain. We present evidence that in a noncytolytic and usually persistent virus infection, high-dose input virus mediates early control of the pathogen due to an efficient induction of an antiviral immune mechanism. From these data, we conclude that immune reactivity, in particular the cytotoxic T-cell response, determines whether the virus is controlled with prevention of the ensuing immunopathological disease or whether a persistent infection is established.

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Antigenic relationship and further characterization of two major Borna disease virus-specific proteins

Cited by 62 publications

References 33 publications

Detection of a novel Borna disease virus-encoded 10 kDa protein in infected cells and tissues.

Detection of a novel Borna disease virus-encoded 10 kDa protein in infected cells and tissues.

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

High-Dose Borna Disease Virus Infection Induces a Nucleoprotein-Specific Cytotoxic T-Lymphocyte Response and Prevention of Immunopathology

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