Bluetongue virus (BTV) was shown to agglutinate human, ovine and porcine erythrocytes. Removal of neuraminic acid (NA) from erythrocytes by neuraminidase prevented their agglutination. Haemagglutination was also inhibited by -acetyl neuraminic acid (NANA), -glycolyl neuraminic acid (NGNA) and -acetyl neuramin-lactose. The ability of BTV to agglutinate trypsin-treated human erythrocytes, which lack the amino-terminal domain and the single -linked oligosaccharide of glycophorin A, suggests that the virus bound to human erythrocytes via NANA-containing, -linked oligosaccharides. Glycoproteins with NA-containing oligosaccharides of known structure such as mucin, fetuin, alpha 1-acid glycoprotein, ovomucoid and ovine, porcine, human and equine glycophorin were examined for their ability to inhibit BTV-mediated agglutination of human, ovine and porcine erythrocytes. All glycoproteins containing NANA- or NGNAα2-6GalNAc were capable of inhibiting the agglutination of human and porcine erythrocytes. Treatment of human erythrocytes with Newcastle disease virus neuraminidase and of porcine erythrocytes with neuraminidase to cleave preferentially the NANA- and NGNAα2-3Gal linkages respectively, were shown to have little effect on the ability of the erythrocytes to be agglutinated by BTV. The results suggested that BTV binds to NANA- and NGNAα2-6GalNAc residues in the -linked oligosaccharides of human and porcine glycophorins respectively and indicated the presence of different binding sites on the virus for erythrocytes from other species.


Article metrics loading...

Loading full text...

Full text loading...


Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error