The carbohydrate structure of the glycoproteins of the paramyxovirus SV5 grown in bovine kidney cells.

The carbohydrate structure of the BIN and F glycoproteins of the paramyxovirus SVS grown in bovine kidney (MDBK) cells has been elucidated by newly developed micromethods. The glycoproteins were purified by chromatography on fetuin coupled to Sepharose and on hydroxylapatite. Extensive aggregation of the F glycoprotein at concentrations > 0.1 mg/ml was reduced by carboxymethylation. The glycopolypeptides I-IN, FI, and Fz contain 3, 3, and 1 carbohydrate chains, respectively, which are linked to asparagine. The oligosaccharides are composed of 1 fucose, 3 mannoses, 4 galactoses, and 2 glucosamines. The reducing end sugar was determined to be glucosamine by gas chromatography after hydrazinolysis, reduction with NaB[%&, and hydrolysis. The linkages were established by methylation analysis. Ten per cent of the carbohydrate chains are esterified with sulfate, which was localized at position 6 of glucosamine by deamination and periodate oxidation of the hydrazinolyzed carbohydrate. Anomeric configurations were determined by chromic oxide oxidation. Aldehydes were detected as constituents of the carbohydrate moieties. The following structure is proposed for the SV5 carbohydrate: