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

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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.

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