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Article: Human bornaviruses and laboratory strains.

Bode, L / Stoyloff, R / Ludwig, H

2000 Volume 355, Issue 9213, Page(s) 1462; author reply 1463

MeSH term(s)	Animals ; Base Sequence/genetics ; Borna Disease/virology ; Borna disease virus/genetics ; DNA, Viral/genetics ; Disease Models, Animal ; Genetic Variation/genetics ; Horse Diseases/virology ; Horses ; Humans ; Mental Disorders/virology ; Mutation/genetics ; Rats
Chemical Substances	DNA, Viral
Language	English
Publishing date	2000-04-22
Publishing country	England
Document type	Comment ; Comparative Study ; Letter
ZDB-ID	3306-6
ISSN	1474-547X ; 0140-6736 ; 0023-7507
ISSN (online)	1474-547X
ISSN	0140-6736 ; 0023-7507
DOI	10.1016/S0140-6736(05)74659-6
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Zs.MG 94: Show issues

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Article: Neutralization of borna disease virus depends upon terminal carbohydrate residues (alpha-D-man, beta-D-GlcNAc) of glycoproteins gp17 and gp94.

Stoyloff, R / Bode, L / Borchers, K / Ludwig, H

Intervirology

1998 Volume 41, Issue 2-3, Page(s) 135–140

Abstract: Borna disease virus (BDV) is an enveloped, nonsegmented, negative-stranded RNA virus that causes infections of the brain in a wide range of animal species and man. The third open reading frame codes for a protein of 17 kD (gp17) that is N-glycosylated ... ...

Abstract	Borna disease virus (BDV) is an enveloped, nonsegmented, negative-stranded RNA virus that causes infections of the brain in a wide range of animal species and man. The third open reading frame codes for a protein of 17 kD (gp17) that is N-glycosylated and contains terminal alpha-D-mannose and N-acetyl-beta-D-glucosamine residues. Rat sera raised against these carbohydrates (anti-sugar antisera) show high in vitro neutralization activity and were capable of precipitating BDV. The neutralizing capacity of sera derived from experimentally BDV-infected rabbits, in turn, decreased after adsorption with those carbohydrates. They partially inhibited infection of primary young rabbit brain cells in a dose-dependent manner. Furthermore, the anti-sugar antisera recognized a second virus-specific glycoprotein with an apparent molecular mass of 94 kD (gp94), providing indirect evidence that gp94 is involved in virus adsorption and/or entry into cells. Neutralization of BDV comprises a complex event and, as shown for the first time, involves the carbohydrate residues of both glycoproteins of BDV.
MeSH term(s)	Acetylglucosamine/chemistry ; Acetylglucosamine/immunology ; Animals ; Antibodies, Viral ; Antigens, Viral/chemistry ; Borna disease virus/chemistry ; Borna disease virus/immunology ; Glycoproteins/chemistry ; Glycoproteins/immunology ; Humans ; In Vitro Techniques ; Mannose/chemistry ; Mannose/immunology ; Neutralization Tests ; Rabbits ; Rats ; Viral Proteins/chemistry ; Viral Proteins/immunology
Chemical Substances	Antibodies, Viral ; Antigens, Viral ; Glycoproteins ; Viral Proteins ; Mannose (PHA4727WTP) ; Acetylglucosamine (V956696549)
Language	English
Publishing date	1998
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	184545-7
ISSN	1423-0100 ; 0300-5526
ISSN (online)	1423-0100
ISSN	0300-5526
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Article: N-glycosylated protein(s) are important for the infectivity of Borna disease virus (BDV).

Stoyloff, R / Briese, T / Borchers, K / Zimmermann, W / Ludwig, H

Archives of virology

1994 Volume 137, Issue 3-4, Page(s) 405–409

Abstract: Tunicamycin inhibited the production of infectious Borna disease virus (BDV) and glycosidase treatment eliminated the infectivity of cell-free virus. A glycoprotein of approximately 17 kDa, found in association with infectious virus, was identified by ... ...

Abstract	Tunicamycin inhibited the production of infectious Borna disease virus (BDV) and glycosidase treatment eliminated the infectivity of cell-free virus. A glycoprotein of approximately 17 kDa, found in association with infectious virus, was identified by Concanavalin A binding.
MeSH term(s)	Borna disease virus/drug effects ; Borna disease virus/pathogenicity ; Cell Line ; Glycoside Hydrolases ; Glycosylation/drug effects ; Humans ; Oligodendroglia/virology ; Tunicamycin/pharmacology ; Viral Envelope Proteins/drug effects ; Viral Envelope Proteins/metabolism ; Viral Envelope Proteins/physiology
Chemical Substances	Viral Envelope Proteins ; Tunicamycin (11089-65-9) ; Glycoside Hydrolases (EC 3.2.1.-)
Language	English
Publishing date	1994
Publishing country	Austria
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	7491-3
ISSN	1432-8798 ; 0304-8608
ISSN (online)	1432-8798
ISSN	0304-8608
DOI	10.1007/bf01309486
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Article: The glycosylated matrix protein of Borna disease virus is a tetrameric membrane-bound viral component essential for infection

Stoyloff, R / Strecker, A / Bode, L / Franke, P / Ludwig, H / Hucho, F

European journal of biochemistry. May 1997. v. 246 (1)

1997

Abstract: Borna disease virus (BDV) is representative of the family of Bornaviridae in the order Mononegavirales (negative-stranded, non-segmented, enveloped RNA viruses). It is the causal agent for Borna disease, characterized as an encephalomyelitis (typical ... ...

Abstract	Borna disease virus (BDV) is representative of the family of Bornaviridae in the order Mononegavirales (negative-stranded, non-segmented, enveloped RNA viruses). It is the causal agent for Borna disease, characterized as an encephalomyelitis (typical form) in a wide variety of domestic animals (from rodents to birds). Recent information shows the involvement of BDV in the pathogenesis of some human psychiatric disorders. The 8.9-kb viral antigenome codes for five major ORF. The third ORF codes for a 16-kDa protein (matrix protein) that is posttranslationally modified, yielding an N-linked glycoprotein. Our data show that the glycosylated matrix protein exists as a stable tetrameric structure detectable either by electrospray ionization or matrix-assisted laser-desorption ionization mass spectrometry. Under native conditions, the tetramer, with a relative molecular mass of 68 kDa, was isolated from a sediment-free brain suspension of a BDV-infected horse. The 68-kDa entity is stable in the presence of ionic and nonionic detergents but dissociates into subunits when heated. We found that the tetrameric matrix protein inhibits in vitro BDV infection in a dose-dependent manner. In contrast to inhibition of BDV infection with hydrophobic carbohydrate derivatives and protein-bound glycoconjugates, the glycosylated matrix protein is a very potent inhibitor of BDV infection, indicating that this protein represents an essential virus-specific membrane component for viral attachment.
Keywords	medicine ; human health and safety ; viral diseases of animals and humans ; animal health ; animal diseases
Language	English
Dates of publication	1997-05
Size	p. 252-257.
Document type	Article
ZDB-ID	3032-6
ISSN	1432-1033 ; 0014-2956
ISSN (online)	1432-1033
ISSN	0014-2956
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Neutralization of Borna Disease Virus Depends upon Terminal Carbohydrate Residues (α-D-Man, β-D-GlcNAc) of Glycoproteins gp17 and gp94

Stoyloff, Roman / Bode, Liv / Borchers, Kerstin / Ludwig, Hanns

Intervirology - International Journal of Basic and Medical Virology

1998 Volume 41, Issue 2-3, Page(s) 135–140

Abstract	Borna disease virus (BDV) is an enveloped, nonsegmented, negative-stranded RNA virus that causes infections of the brain in a wide range of animal species and man. The third open reading frame codes for a protein of 17 kD (gp17) that is N-glycosylated and contains terminal α-D-mannose and N-acetyl-β-D-glucosamine residues. Rat sera raised against these carbohydrates (anti-sugar antisera) show high in vitro neutralization activity and were capable of precipitating BDV. The neutralizing capacity of sera derived from experimentally BDV-infected rabbits, in turn, decreased after adsorption with those carbohydrates. They partially inhibited infection of primary young rabbit brain cells in a dose-dependent manner. Furthermore, the anti-sugar antisera recognized a second virus-specific glycoprotein with an apparent molecular mass of 94 kD (gp94), providing indirect evidence that gp94 is involved in virus adsorption and/or entry into cells. Neutralization of BDV comprises a complex event and, as shown for the first time, involves the carbohydrate residues of both glycoproteins of BDV.
Keywords	Borna disease virus ; M protein ; G protein ; Glycoproteins ; Virus surface ; Neutralization
Language	English
Publisher	S. Karger AG
Publishing place	Basel
Publishing country	Switzerland
Document type	Article ; Online
ZDB-ID	184545-7
ISSN	1423-0100 ; 0300-5526 ; 0300-5526
ISSN (online)	1423-0100
ISSN	0300-5526
DOI	10.1159/000024926
Database	Karger publisher's database

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Zs.A 1040: Show issues

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Article: Amantadine and human Borna disease virus in vitro and in vivo in an infected patient with bipolar depression.

Bode, L / Dietrich, D E / Stoyloff, R / Emrich, H M / Ludwig, H

Lancet (London, England)

1997 Volume 349, Issue 9046, Page(s) 178–179

MeSH term(s)	Aged ; Amantadine/therapeutic use ; Animals ; Antiviral Agents/therapeutic use ; Bipolar Disorder/complications ; Bipolar Disorder/drug therapy ; Borna Disease/complications ; Borna Disease/drug therapy ; Borna disease virus/drug effects ; Female ; Humans ; Rabbits
Chemical Substances	Antiviral Agents ; Amantadine (BF4C9Z1J53)
Language	English
Publishing date	1997-01-18
Publishing country	England
Document type	Case Reports ; Letter
ZDB-ID	3306-6
ISSN	1474-547X ; 0140-6736 ; 0023-7507
ISSN (online)	1474-547X
ISSN	0140-6736 ; 0023-7507
DOI	10.1016/S0140-6736(05)60979-8
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Article: The glycosylated matrix protein of Borna disease virus is a tetrameric membrane-bound viral component essential for infection.

Stoyloff, R / Strecker, A / Bode, L / Franke, P / Ludwig, H / Hucho, F

European journal of biochemistry

1997 Volume 246, Issue 1, Page(s) 252–257

Abstract	Borna disease virus (BDV) is representative of the family of Bornaviridae in the order Mononegavirales (negative-stranded, non-segmented, enveloped RNA viruses). It is the causal agent for Borna disease, characterized as an encephalomyelitis (typical form) in a wide variety of domestic animals (from rodents to birds). Recent information shows the involvement of BDV in the pathogenesis of some human psychiatric disorders. The 8.9-kb viral antigenome codes for five major ORF. The third ORF codes for a 16-kDa protein (matrix protein) that is posttranslationally modified, yielding an N-linked glycoprotein. Our data show that the glycosylated matrix protein exists as a stable tetrameric structure detectable either by electrospray ionization or matrix-assisted laser-desorption ionization mass spectrometry. Under native conditions, the tetramer, with a relative molecular mass of 68 kDa, was isolated from a sediment-free brain suspension of a BDV-infected horse. The 68-kDa entity is stable in the presence of ionic and nonionic detergents but dissociates into subunits when heated. We found that the tetrameric matrix protein inhibits in vitro BDV infection in a dose-dependent manner. In contrast to inhibition of BDV infection with hydrophobic carbohydrate derivatives and protein-bound glycoconjugates, the glycosylated matrix protein is a very potent inhibitor of BDV infection, indicating that this protein represents an essential virus-specific membrane component for viral attachment.
MeSH term(s)	Animals ; Blotting, Western ; Borna disease virus/chemistry ; Borna disease virus/pathogenicity ; Brain/virology ; Cells, Cultured ; Electrophoresis, Gel, Two-Dimensional ; Enzyme-Linked Immunosorbent Assay ; Glycoproteins/chemistry ; Glycoproteins/isolation & purification ; Glycosylation ; Horses ; Protein Conformation ; Protein Denaturation ; Rabbits ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Viral Matrix Proteins/chemistry ; Viral Matrix Proteins/isolation & purification ; Viral Matrix Proteins/physiology
Chemical Substances	Glycoproteins ; Viral Matrix Proteins
Language	English
Publishing date	1997-05-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3032-6
ISSN	1432-1033 ; 0014-2956
ISSN (online)	1432-1033
ISSN	0014-2956
DOI	10.1111/j.1432-1033.1997.t01-2-00252.x
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Article: Borna disease virus-specific circulating immune complexes, antigenemia, and free antibodies--the key marker triplet determining infection and prevailing in severe mood disorders.

Bode, L / Reckwald, P / Severus, W E / Stoyloff, R / Ferszt, R / Dietrich, D E / Ludwig, H

Molecular psychiatry

2001 Volume 6, Issue 4, Page(s) 481–491

Abstract: Borna disease virus (BDV), a unique genetically highly conserved RNA virus (Bornaviridae; Mononegavirales), preferentially targets neurons of limbic structures causing behavioral abnormalities in animals. Markers and virus in patients with affective ... ...

Abstract	Borna disease virus (BDV), a unique genetically highly conserved RNA virus (Bornaviridae; Mononegavirales), preferentially targets neurons of limbic structures causing behavioral abnormalities in animals. Markers and virus in patients with affective disorders and schizophrenia have raised worldwide interest. A persistent infection was suggestive from follow-up studies, but inconstant detectability weakened a possible linkage.This study for the first time discloses that detection gaps are caused by BDV-specific circulating immune complexes (CIC), and their interplay with free antibodies and plasma antigens (p40/p24). Screening 3000 sera each from human and equine patients over the past 4 years by new enzyme immunoassays (EIAs) revealed that BDV-CICs indicate 10 times higher infection rates (up to 30% in controls, up to 100% in patients) than did previous serology. Persistence of high amounts of CICs and plasma antigens correlates with severity of depression. Even BDV RNA could be detected in plasma samples with strong antigenemia. Our discovery not only explains the course of persistent infection, but offers novel easy-to-use diagnostic tools by which new insights into BDV-related etiopathogenesis of disease and epidemiology are possible.
MeSH term(s)	Adult ; Aged ; Aged, 80 and over ; Animals ; Antibodies, Viral/blood ; Antigen-Antibody Complex/blood ; Antigens, Viral/blood ; Bipolar Disorder/blood ; Bipolar Disorder/immunology ; Borna Disease/blood ; Borna Disease/genetics ; Borna Disease/immunology ; Borna disease virus/immunology ; Depressive Disorder/blood ; Depressive Disorder/immunology ; Female ; Horse Diseases/blood ; Horses/blood ; Horses/virology ; Humans ; Male ; Middle Aged ; Mood Disorders/blood ; Mood Disorders/immunology
Chemical Substances	Antibodies, Viral ; Antigen-Antibody Complex ; Antigens, Viral
Language	English
Publishing date	2001-07
Publishing country	England
Document type	Journal Article ; Multicenter Study ; Research Support, Non-U.S. Gov't
ZDB-ID	1330655-8
ISSN	1476-5578 ; 1359-4184
ISSN (online)	1476-5578
ISSN	1359-4184
DOI	10.1038/sj.mp.4000909
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Article: N-glycosylated protein(s) are important for the infectivity of Borna disease virus (BDV)

Stoyloff, R / Briese, T / Borchers, K / Zimmermann, W / Ludwig, H

Archives of virology. 1994. v. 137 (3/4)

1994

Abstract	Tunicamycin inhibited the production of infectious Borna disease virus (BDV) and glycosidase treatment eliminated the infectivity of cell-free virus. A glycoprotein of approximately 17 kDa, found in association with infectious virus, was identified by Concanavalin A binding.
Keywords	viruses ; Borna disease virus ; glycoproteins ; tunicamycin ; glycosyltransferases
Language	English
Size	p. 405-409.
Document type	Article
ZDB-ID	7491-3
ISSN	1432-8798 ; 0304-8608
ISSN (online)	1432-8798
ISSN	0304-8608
Database	NAL-Catalogue (AGRICOLA)

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Z 70/128: Show issues

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Book ; Audio / Video ; Online: A new permanent young rabbit spleen (YRS) cell line - an efficient tool to study Bornavirus isolates of human and animal origin

Ludwig, H. / Leiskau, C. / Reckwald, P. / Riebe, Roland / Rantam, F. / Stoyloff, R. / Bode, L.

2001

Language	English
Publishing date	2001-03-14
Publishing country	de
Document type	Book ; Audio / Video ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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