Neutralization of borna disease virus depends upon terminal carbohydrate residues (alpha-D-man, beta-D-GlcNAc) of glycoproteins gp17 and gp94.
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.
Stoyloff
R
R
Institut für Virologie, Freie Universität Berlin, Berlin, Deutschland.
Bode
L
L
Borchers
K
K
Ludwig
H
H
D000117:Acetylglucosamine / Q000737:chemistry / Q000276:immunology; D000818:Animals; D000914:Antibodies, Viral; D000956:Antigens, Viral / Q000737:chemistry; D001891:Borna disease virus / Q000737:chemistry / Q000276:immunology*; D006023:Glycoproteins / Q000737:chemistry / Q000276:immunology*; D006801:Humans; D066298:In Vitro Techniques; D008358:Mannose / Q000737:chemistry / Q000276:immunology; D009500:Neutralization Tests; D011817:Rabbits; D051381:Rats; D014764:Viral Proteins / Q000737:chemistry / Q000276:immunology*
D000914:Antibodies, Viral; D000956:Antigens, Viral; D006023:Glycoproteins; D014764:Viral Proteins; D008358:Mannose; D000117:Acetylglucosamine