scholarly journals Expression and Characterization of the Borna Disease Virus Polymerase

2000 ◽  
Vol 74 (9) ◽  
pp. 4425-4428 ◽  
Author(s):  
Michelle Portlance Walker ◽  
Ingo Jordan ◽  
Thomas Briese ◽  
Nicole Fischer ◽  
W. Ian Lipkin
Keyword(s):  
Disease Virus ◽  
Genomic Sequence ◽  
Transcription Unit ◽  
Open Reading Frame ◽  
Upstream Open Reading Frame ◽  
Viral Polymerase ◽  
Borna Disease Virus ◽  
Reading Frame ◽  
Borna Disease

ABSTRACT Borna disease virus is the prototype of a new family,Bornaviridae, within the order Mononegavirales, that is characterized by nuclear transcription, splicing, low level replication, and neurotropism. The products of five open reading frames predicted from the genomic sequence have been confirmed; however, expression of the sixth, corresponding to the putative viral polymerase (L), has not been demonstrated. Here, we describe expression and characterization of a 190-kDa protein proposed to represent L. Expression of this protein from the third transcription unit of the viral genome is dependent on a splicing event that fuses a small upstream open reading frame in frame with the larger downstream continuous open reading frame. The protein is detected by serum antibodies from infected rats and is present in the nucleus, where it colocalizes with the phosphoprotein. L is also shown to be phosphorylated by cellular kinases and to interact with the viral phosphoprotein in coimmunoprecipitation studies. These findings are consistent with the identity of the 190-kDa protein as the viral polymerase and provide insights and describe reagents that will be useful for Bornavirus molecular biology and pathobiology.

scholarly journals Nuclear Localization of the Protein from the Open Reading Frame x1 of the Borna Disease Virus Was through Interactions with the Viral Nucleoprotein

Virology ◽  
1999 ◽  
Vol 258 (1) ◽  
pp. 65-72 ◽  
Author(s):  
Tahir H. Malik ◽  
Takeshi Kobayashi ◽  
Mimi Ghosh ◽  
Masahiko Kishi ◽  
Patrick K. Lai
Keyword(s):  
Disease Virus ◽  
Nuclear Localization ◽  
Open Reading Frame ◽  
Borna Disease Virus ◽  
Reading Frame ◽  
Borna Disease

Processing of the Borna Disease Virus Glycoprotein gp94 by the Subtilisin-Like Endoprotease Furin

1998 ◽  
Vol 72 (5) ◽  
pp. 4528-4533 ◽  
Author(s):  
Jürgen A. Richt ◽  
Thomas Fürbringer ◽  
Andreas Koch ◽  
Isolde Pfeuffer ◽  
Christiane Herden ◽  
...  
Keyword(s):  
Biological Activity ◽  
Molecular Mass ◽  
Disease Virus ◽  
Open Reading Frame ◽  
Cleavage Sites ◽  
Precursor Molecule ◽  
Borna Disease Virus ◽  
Calculated Molecular Mass ◽  
Reading Frame ◽  
Borna Disease

ABSTRACT Open reading frame IV (ORF-IV) of Borna disease virus (BDV) encodes a protein with a calculated molecular mass of ca. 57 kDa (p57), which increases after N glycosylation to 94 kDa (gp94). The unglycosylated and glycosylated proteins are proteolytically cleaved by the subtilisin-like protease furin. Furin most likely recognizes one of three potential cleavage sites, namely, an arginine at position 249 of the ORF-IV gene product. The furin inhibitor decRVKRcmk decreases the production of infectious BDV significantly, indicating that proteolytic cleavage of the gp94 precursor molecule is necessary for the full biological activity of the BDV glycoprotein.

scholarly journals Open Reading Frame III of Borna Disease Virus Encodes a Nonglycosylated Matrix Protein

2001 ◽  
Vol 75 (24) ◽  
pp. 12098-12104 ◽  
Author(s):  
Ina Kraus ◽  
Markus Eickmann ◽  
Simone Kiermayer ◽  
Hanno Scheffczik ◽  
Manuela Fluess ◽  
...  
Keyword(s):  
Disease Virus ◽  
Matrix Protein ◽  
Consensus Sequence ◽  
Integral Membrane Protein ◽  
Open Reading Frame ◽  
Membrane Topology ◽  
Homologous Proteins ◽  
Borna Disease Virus ◽  
Reading Frame ◽  
Borna Disease

ABSTRACT The open reading frame III of Borna disease virus (BDV) codes for a protein with a mass of 16 kDa, named p16 or BDV-M. p16 was described as an N-glycosylated protein in several previous publications and therefore was termed gp18, although the amino acid sequence of p16 does not contain any regular consensus sequence for N glycosylation. We examined glycosylation of p16 and studied its membrane topology using antisera raised against peptides, which comprise the N and the C termini. Neither an N- nor a C-terminal peptide is cleaved from p16 during maturation. Neither deglycosylation of p16 by endoglycosidases nor binding of lectin to p16 was detectable. Introduction of typical N-glycosylation sites at the proposed sites of p16 failed in carbohydrate attachment. Flotation experiments with membranes of BDV-infected cells on density gradients revealed that p16 is not an integral membrane protein, since it can be dissociated from membranes. Our experimental data strongly suggest that p16 is a typical nonglycosylated matrix protein associated at the inner surface of the viral membrane, as is true for homologous proteins of other members of the Mononegavirales order.

scholarly journals Characterization of an Unusual Importin α Binding Motif in the Borna Disease Virus p10 Protein That Directs Nuclear Import

2002 ◽  
Vol 277 (14) ◽  
pp. 12151-12157 ◽  
Author(s):  
Thorsten Wolff ◽  
Gunhild Unterstab ◽  
Gudrun Heins ◽  
Juergen A. Richt ◽  
Michael Kann
Keyword(s):  
Disease Virus ◽  
Nuclear Import ◽  
Binding Motif ◽  
Borna Disease Virus ◽  
Importin Α ◽  
Borna Disease

Sequence characterization of human Borna disease virus

1996 ◽  
Vol 44 (1) ◽  
pp. 33-44 ◽  
Author(s):  
Juan Carlos de la Torre ◽  
Liv Bode ◽  
Ralf Dürrwald ◽  
Beatrice Cubitt ◽  
Hanns Ludwig
Keyword(s):  
Disease Virus ◽  
Borna Disease Virus ◽  
Sequence Characterization ◽  
Borna Disease

scholarly journals Isolation and Characterization of a New Subtype of Borna Disease Virus

2000 ◽  
Vol 74 (12) ◽  
pp. 5655-5658 ◽  
Author(s):  
Norbert Nowotny ◽  
Jolanta Kolodziejek ◽  
Christian O. Jehle ◽  
Angelika Suchy ◽  
Peter Staeheli ◽  
...  
Keyword(s):  
Disease Virus ◽  
Single Type ◽  
The Novel ◽  
Borna Disease Virus ◽  
Diagnostic Assays ◽  
Isolation And Characterization ◽  
First Time ◽  
Reference Strains ◽  
Borna Disease

ABSTRACT Borna disease virus (BDV), the causative agent of severe meningoencephalitis in a wide variety of animal species, has been considered to be genetically invariable and to form a single type within the genus Bornavirus of the familyBornaviridae. BDV infections are of particular interest, because for the first time a virus infection appears to be linked to human psychiatric disorders. We now describe a new subtype of BDV isolated from a horse which was euthanatized due to severe, incurable neurological disease. The nucleotide sequence of this new strain, named No/98, differs from the reference strains by more than 15%, and the subtype is difficult to detect by standard reverse transcriptase PCR protocols. The nucleotide exchanges of the novel BDV isolate have surprisingly little effect on the primary structures of most viral proteins, with the notable exception of the X protein (p10), which is only 81% identical to its counterpart in reference strains. Our data indicate that the genome of BDV is far more variable than previously assumed and that naturally occurring subtypes may escape detection by currently used diagnostic assays.

scholarly journals Characterization of Borna disease virus p56 protein, a surface glycoprotein involved in virus entry.

1997 ◽  
Vol 71 (4) ◽  
pp. 3208-3218 ◽  
Author(s):  
D Gonzalez-Dunia ◽  
B Cubitt ◽  
F A Grasser ◽  
J C de la Torre
Keyword(s):  
Disease Virus ◽  
Virus Entry ◽  
Protein A ◽  
Surface Glycoprotein ◽  
Borna Disease Virus ◽  
Borna Disease

scholarly journals Infection with Borna Disease Virus: Molecular and Immunobiological Characterization of the Agent

1992 ◽  
Vol 14 (6) ◽  
pp. 1240-1250 ◽  
Author(s):  
J. A. Richt ◽  
S. VandeWoude ◽  
M. C. Zink ◽  
J. E. Clements ◽  
S. Herzog ◽  
...  
Keyword(s):  
Disease Virus ◽  
Borna Disease Virus ◽  
Borna Disease
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