Specific changes in the oligosaccharide moieties of VSV grown in different lectin-resistant CHO cells

Margaret A. Robertson; James R. Etchison; James S. Robertson; Donald F. Summers; Pamela Stanley

doi:10.1016/0092-8674(78)90325-2

Specific changes in the oligosaccharide moieties of VSV grown in different lectin-resistant CHO cells

Margaret A. Robertson, James R. Etchison, James S. Robertson, Donald F. Summers, Pamela Stanley

Research output: Contribution to journal › Article › peer-review

75 Scopus citations

Abstract

The carbohydrate moieties of the G glycoprotein of vesicular stomatitis virus (VSV) grown in three distinct lectin-resistant (Lec^R) Chinese hamster ovary (CHO) cell lines have been compared by fine structural analysis of radiolabeled glycopeptides. The mutant Wga^RIII, selected for resistance to wheat germ agglutinin (WGA), produces VSV containing G glycoprotein specifically lacking in sialic acid. The mutant Pha^RI, selected for resistance to phytohemagglutinin (PHA) and previously shown to lack a particular glycoprotein N-acetyl-glucosaminyl-transferase activity, produces VSV containing G glycoprotein specifically lacking terminal N-acetylglucosamine-galactose-sialic acid sequences and possessing an increased number of mannose residues in the "core" region of its carbohydrate moieties. The mutant Pha^RIConA^RII, a "double" mutant selected from Pha^RI cells for resistance to concanavalin A (ConA), produces VSV containing G glycoprotein with a further alteration in the mannose residues of the "core" oligosaccharide region. We discuss the relevance of these findings to the mechanisms of glycoprotein biosynthesis in mammalian cells and to the biochemical bases of lectin resistance in CHO cells.

Original language	English (US)
Pages (from-to)	515-526
Number of pages	12
Journal	Cell
Volume	13
Issue number	3
DOIs	https://doi.org/10.1016/0092-8674(78)90325-2
State	Published - Mar 1978
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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title = "Specific changes in the oligosaccharide moieties of VSV grown in different lectin-resistant CHO cells",

abstract = "The carbohydrate moieties of the G glycoprotein of vesicular stomatitis virus (VSV) grown in three distinct lectin-resistant (LecR) Chinese hamster ovary (CHO) cell lines have been compared by fine structural analysis of radiolabeled glycopeptides. The mutant WgaRIII, selected for resistance to wheat germ agglutinin (WGA), produces VSV containing G glycoprotein specifically lacking in sialic acid. The mutant PhaRI, selected for resistance to phytohemagglutinin (PHA) and previously shown to lack a particular glycoprotein N-acetyl-glucosaminyl-transferase activity, produces VSV containing G glycoprotein specifically lacking terminal N-acetylglucosamine-galactose-sialic acid sequences and possessing an increased number of mannose residues in the {"}core{"} region of its carbohydrate moieties. The mutant PhaRIConARII, a {"}double{"} mutant selected from PhaRI cells for resistance to concanavalin A (ConA), produces VSV containing G glycoprotein with a further alteration in the mannose residues of the {"}core{"} oligosaccharide region. We discuss the relevance of these findings to the mechanisms of glycoprotein biosynthesis in mammalian cells and to the biochemical bases of lectin resistance in CHO cells.",

author = "Robertson, {Margaret A.} and Etchison, {James R.} and Robertson, {James S.} and Summers, {Donald F.} and Pamela Stanley",

note = "Funding Information: This work was supported by a grant from the NIH and grants from the NSF. J.R.E. was supported by a postdoctoral fellowship from the American Cancer Society. J.S.R. was supported by a NATO postdoctoral fellowship from the Science Research Council, London, England. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.",

year = "1978",

month = mar,

doi = "10.1016/0092-8674(78)90325-2",

language = "English (US)",

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pages = "515--526",

journal = "Cell",

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number = "3",

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T1 - Specific changes in the oligosaccharide moieties of VSV grown in different lectin-resistant CHO cells

AU - Robertson, Margaret A.

AU - Etchison, James R.

AU - Robertson, James S.

AU - Summers, Donald F.

AU - Stanley, Pamela

N1 - Funding Information: This work was supported by a grant from the NIH and grants from the NSF. J.R.E. was supported by a postdoctoral fellowship from the American Cancer Society. J.S.R. was supported by a NATO postdoctoral fellowship from the Science Research Council, London, England. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

PY - 1978/3

Y1 - 1978/3

N2 - The carbohydrate moieties of the G glycoprotein of vesicular stomatitis virus (VSV) grown in three distinct lectin-resistant (LecR) Chinese hamster ovary (CHO) cell lines have been compared by fine structural analysis of radiolabeled glycopeptides. The mutant WgaRIII, selected for resistance to wheat germ agglutinin (WGA), produces VSV containing G glycoprotein specifically lacking in sialic acid. The mutant PhaRI, selected for resistance to phytohemagglutinin (PHA) and previously shown to lack a particular glycoprotein N-acetyl-glucosaminyl-transferase activity, produces VSV containing G glycoprotein specifically lacking terminal N-acetylglucosamine-galactose-sialic acid sequences and possessing an increased number of mannose residues in the "core" region of its carbohydrate moieties. The mutant PhaRIConARII, a "double" mutant selected from PhaRI cells for resistance to concanavalin A (ConA), produces VSV containing G glycoprotein with a further alteration in the mannose residues of the "core" oligosaccharide region. We discuss the relevance of these findings to the mechanisms of glycoprotein biosynthesis in mammalian cells and to the biochemical bases of lectin resistance in CHO cells.

AB - The carbohydrate moieties of the G glycoprotein of vesicular stomatitis virus (VSV) grown in three distinct lectin-resistant (LecR) Chinese hamster ovary (CHO) cell lines have been compared by fine structural analysis of radiolabeled glycopeptides. The mutant WgaRIII, selected for resistance to wheat germ agglutinin (WGA), produces VSV containing G glycoprotein specifically lacking in sialic acid. The mutant PhaRI, selected for resistance to phytohemagglutinin (PHA) and previously shown to lack a particular glycoprotein N-acetyl-glucosaminyl-transferase activity, produces VSV containing G glycoprotein specifically lacking terminal N-acetylglucosamine-galactose-sialic acid sequences and possessing an increased number of mannose residues in the "core" region of its carbohydrate moieties. The mutant PhaRIConARII, a "double" mutant selected from PhaRI cells for resistance to concanavalin A (ConA), produces VSV containing G glycoprotein with a further alteration in the mannose residues of the "core" oligosaccharide region. We discuss the relevance of these findings to the mechanisms of glycoprotein biosynthesis in mammalian cells and to the biochemical bases of lectin resistance in CHO cells.

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Specific changes in the oligosaccharide moieties of VSV grown in different lectin-resistant CHO cells

Abstract

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