O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus

David Johnson, Patricia G. Spear

Research output: Contribution to journalArticle

138 Citations (Scopus)

Abstract

The O-linked oligosaccharides on mature forms of herpes simplex virus type 1 (HSV1) glycoproteins were characterized, and were found to account largely for the lower electrophoretic mobilities of these forms relative to the mobilities of immature forms. Other posttranslational modifications of HSV1 glycoproteins (designated gB, gC, gD and gE) were related temporally to the discrete shifts in electrophoretic mobilities that signal acquisition of the O-linked oligosaccharides. Fatty acid acylation (principally of gE) could be detected just prior to the shifts, whereas conversion of high-mannosetype N-linked oligosaccharides to the complex type occurred coincident with the shifts. The addition of O-linked oligosaccharides did not occur in cells treated with the ionophore monensin or in a ricinresistant cell line defective in the processing of N-linked oligosaccharides. We conclude that extension of O-linked oligosaccharide chains on HSV1 glycoproteins, and probably also attachment of the first O-linked sugars, occurs as a late posttranslational modification in the Golgi apparatus.

Original languageEnglish (US)
Pages (from-to)987-997
Number of pages11
JournalCell
Volume32
Issue number3
DOIs
StatePublished - 1983
Externally publishedYes

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Golgi Apparatus
Simplexvirus
Oligosaccharides
Viruses
Glycoproteins
Human Herpesvirus 1
Electrophoretic mobility
Post Translational Protein Processing
Monensin
Acylation
Ionophores
Sugars
Fatty Acids
Cells
Cell Line
Processing

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus. / Johnson, David; Spear, Patricia G.

In: Cell, Vol. 32, No. 3, 1983, p. 987-997.

Research output: Contribution to journalArticle

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AB - The O-linked oligosaccharides on mature forms of herpes simplex virus type 1 (HSV1) glycoproteins were characterized, and were found to account largely for the lower electrophoretic mobilities of these forms relative to the mobilities of immature forms. Other posttranslational modifications of HSV1 glycoproteins (designated gB, gC, gD and gE) were related temporally to the discrete shifts in electrophoretic mobilities that signal acquisition of the O-linked oligosaccharides. Fatty acid acylation (principally of gE) could be detected just prior to the shifts, whereas conversion of high-mannosetype N-linked oligosaccharides to the complex type occurred coincident with the shifts. The addition of O-linked oligosaccharides did not occur in cells treated with the ionophore monensin or in a ricinresistant cell line defective in the processing of N-linked oligosaccharides. We conclude that extension of O-linked oligosaccharide chains on HSV1 glycoproteins, and probably also attachment of the first O-linked sugars, occurs as a late posttranslational modification in the Golgi apparatus.

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