Glycoproteins D1 (gD1) and D2 (gD2) of herpes simplex virus type 1 and type 2, respectively, were purified from infected HEp-2 cells labelled with [H]glucosamine for 14 h followed by a 3 h chase using HD1 monoclonal antibody linked to Sepharose. -linked oligosaccharides were found to be present in both glycoproteins. The identification of -acetyl [H]galactosaminitol as the major labelled component in the oligosaccharides generated by mild alkaline borohydride treatment demonstrated that these chains have -acetylgalactosamine at the reducing end. These oligosaccharides consist of mono- and disialylated species with a predominance of the latter species in gD1. Size analysis and radioactive amino sugar composition strongly suggest a structure in which the galactosyl--acetylgalactosamine core is substituted with one or two sialic acid residues. In terms of [H]glucosamine-derived radioactivity, -linked oligosaccharides are less represented than -linked oligosaccharides. The -linked oligosaccharide number determination showed that gD1 and gD2 carry two and three chains, respectively.


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