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10.1159/000024926

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9820849!ä!9820849

suck abstract from ncbi


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pmid9820849      Intervirology 1998 ; 41 (2-3): 135-40
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  • Neutralization of borna disease virus depends upon terminal carbohydrate residues (alpha-D-man, beta-D-GlcNAc) of glycoproteins gp17 and gp94 #MMPMID9820849
  • Stoyloff R; Bode L; Borchers K; Ludwig H
  • Intervirology 1998[]; 41 (2-3): 135-40 PMID9820849show ga
  • 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.
  • |Acetylglucosamine/chemistry/immunology[MESH]
  • |Animals[MESH]
  • |Antibodies, Viral[MESH]
  • |Antigens, Viral/chemistry[MESH]
  • |Borna disease virus/chemistry/*immunology[MESH]
  • |Glycoproteins/chemistry/*immunology[MESH]
  • |Humans[MESH]
  • |In Vitro Techniques[MESH]
  • |Mannose/chemistry/immunology[MESH]
  • |Neutralization Tests[MESH]
  • |Rabbits[MESH]
  • |Rats[MESH]


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