Glycosylation sites of influenza viral glycoproteins: characterization of tryptic glycopeptides from the A/USSR(H1N1) hemagglutinin glycoprotein

S Basak, D G Pritchard, A S Bhown, R W Compans
1981 Journal of Virology  
Glycosylated tryptic peptides of the hemagglutinin (HA) glycoprotein of influenza A/USSR/90/77(HlN1) virus were separated by a combination of ion-exchange chromatography and gel filtration. Seven different glycosylated tryptic peptide classes were obtained from the HAl polypeptide, and only one glycosylated peptide was obtained from the HA2 polypeptide. Several of the tryptic fragments of HAl and the HA2 glycopeptides were sulfated. The nature of the carbohydrate chain in each of the
more » ... d tryptic peptides was determined from observations of the incorporation of different sugar precursors and susceptibility to cleavage by the enzyme endoglycosidase H and by compositional analysis by gas chromatography. Such analyses showed that three types of carbohydrate chains were present in HAl (type I [complex], type II [high mannose], and hybrid type), whereas HA2 contained only type I oligosaccharide chains. The amino acid composition of each of the glycosylated tryptic peptides was also determined.
doi:10.1128/jvi.37.2.549-558.1981 fatcat:y6aw7bdn2bhexcmubdwzteshgi