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PMID: 6299584 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Cell ·Vol. 32 ·No. 3 ·1983-03-00 ·Pages 987-97

Johnson DC, Spear PG

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-mannose-type 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 ricin-resistant 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.

MeSH Terms
Animals Cell Line Drug Resistance Electrophoresis, Polyacrylamide Gel Glycoproteins/analysis Golgi Apparatus/metabolism Hydrolysis Lectins/pharmacology Mice Neuraminidase/metabolism Oligosaccharides/analysis Protein Processing, Post-Translational Simplexvirus/analysis
Chemicals
Glycoproteins Lectins Oligosaccharides Neuraminidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Johnson D C
Spear P G
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51 references, click to expand
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Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
1983-03-00
Pages
987-97
Language
English
Region
United States
NLM ID
0413066
PMCID
PMC7133230
Subset
IM
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