Immature and mature forms of glycoprotein gC were purified by immunoadsorbent from herpes simplex virus type 1-infected BHK cells labeled with [3H]mannose for a 20-mim pulse or for 11 h followed by a 3-h chase. The nature of N-asparagine-linked oligosaccharides carried by the immature form, pgC (molecular weight = 92,000), and the mature gC (molecular weight = 120,000) has been investigated. All pronase-digested glycopeptides of pgC were susceptible to endo-β-N-acetylglycosaminidase H treatment; thus they have a high-mannose structure. Using thin-layer chromatography to separate endo-β-N-acetylglycosaminidase H-cleaved oligosaccharides, polymannosyl chains of different size, ranging from Man9GlcNAc to Man5GlcNAc, were separated. The major components were Man8GlcNAc and Man7GlcNAc, suggesting that pgC labeled in a 20-min pulse represents the form of glycoprotein already routed to the Golgi apparatus. Analysis of glycopeptides of mature gC showed that the majority (95%) of N-linked glycans were converted to complex-type glycans. Ion-exchange chromatography and affinity chromatography on concanavalin A-Sepharose and leucoagglutinin-agarose revealed that diantennary and triantennary chains were not fully sialylated. The high heterogeneity of complex-type chains found in mature gC may be related to the high number of N-glycosylation sites of the glycoprotein as predicted by DNA sequencing studies.

Serafini-Cessi F., Dall'Olio F., Pereira L., Campadelli-Fiume G. (1984). Processing of N-linked oligosaccharides from precursor- to mature-form herpes simplex virus type 1 glycoprotein gC. JOURNAL OF VIROLOGY, 51(3), 838-844 [10.1128/jvi.51.3.838-844.1984].

Processing of N-linked oligosaccharides from precursor- to mature-form herpes simplex virus type 1 glycoprotein gC

Dall'Olio F.;Campadelli-Fiume G.
1984

Abstract

Immature and mature forms of glycoprotein gC were purified by immunoadsorbent from herpes simplex virus type 1-infected BHK cells labeled with [3H]mannose for a 20-mim pulse or for 11 h followed by a 3-h chase. The nature of N-asparagine-linked oligosaccharides carried by the immature form, pgC (molecular weight = 92,000), and the mature gC (molecular weight = 120,000) has been investigated. All pronase-digested glycopeptides of pgC were susceptible to endo-β-N-acetylglycosaminidase H treatment; thus they have a high-mannose structure. Using thin-layer chromatography to separate endo-β-N-acetylglycosaminidase H-cleaved oligosaccharides, polymannosyl chains of different size, ranging from Man9GlcNAc to Man5GlcNAc, were separated. The major components were Man8GlcNAc and Man7GlcNAc, suggesting that pgC labeled in a 20-min pulse represents the form of glycoprotein already routed to the Golgi apparatus. Analysis of glycopeptides of mature gC showed that the majority (95%) of N-linked glycans were converted to complex-type glycans. Ion-exchange chromatography and affinity chromatography on concanavalin A-Sepharose and leucoagglutinin-agarose revealed that diantennary and triantennary chains were not fully sialylated. The high heterogeneity of complex-type chains found in mature gC may be related to the high number of N-glycosylation sites of the glycoprotein as predicted by DNA sequencing studies.
1984
Serafini-Cessi F., Dall'Olio F., Pereira L., Campadelli-Fiume G. (1984). Processing of N-linked oligosaccharides from precursor- to mature-form herpes simplex virus type 1 glycoprotein gC. JOURNAL OF VIROLOGY, 51(3), 838-844 [10.1128/jvi.51.3.838-844.1984].
Serafini-Cessi F.; Dall'Olio F.; Pereira L.; Campadelli-Fiume G.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/903364
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