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Identification and characterization of a mouse cell mutant defective in the intracellular transport of glycoproteins

We have isolated a mutant line of mouse L cells, termed gro29, in which the growth of herpes simplex virus (HSV) and vesicular stomatitis virus (VSV) is defective. The block occurs late in the infectious cycle of both viruses. We demonstrate that HSV and VSV enter gro29 cells normally, negotiate the...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1987
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114779/
https://www.ncbi.nlm.nih.gov/pubmed/3040769
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description We have isolated a mutant line of mouse L cells, termed gro29, in which the growth of herpes simplex virus (HSV) and vesicular stomatitis virus (VSV) is defective. The block occurs late in the infectious cycle of both viruses. We demonstrate that HSV and VSV enter gro29 cells normally, negotiate the early stages of infection, yet are impaired at a late stage of virus maturation. During VSV infection of the mutant cell line, intracellular transport of its glycoprotein (G protein) is slowed. Pulse-chase experiments showed that oligosaccharide processing is impeded, and immunofluorescence localization revealed an accumulation of G protein in a juxtanuclear region that contains the Golgi complex. We conclude that export of newly made glycoproteins is defective in gro29 cells, and speculate that this defect may reflect a lesion in the glycoprotein transport apparatus.
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spelling pubmed-21147792008-05-01 Identification and characterization of a mouse cell mutant defective in the intracellular transport of glycoproteins J Cell Biol Articles We have isolated a mutant line of mouse L cells, termed gro29, in which the growth of herpes simplex virus (HSV) and vesicular stomatitis virus (VSV) is defective. The block occurs late in the infectious cycle of both viruses. We demonstrate that HSV and VSV enter gro29 cells normally, negotiate the early stages of infection, yet are impaired at a late stage of virus maturation. During VSV infection of the mutant cell line, intracellular transport of its glycoprotein (G protein) is slowed. Pulse-chase experiments showed that oligosaccharide processing is impeded, and immunofluorescence localization revealed an accumulation of G protein in a juxtanuclear region that contains the Golgi complex. We conclude that export of newly made glycoproteins is defective in gro29 cells, and speculate that this defect may reflect a lesion in the glycoprotein transport apparatus. The Rockefeller University Press 1987-08-01 /pmc/articles/PMC2114779/ /pubmed/3040769 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Identification and characterization of a mouse cell mutant defective in the intracellular transport of glycoproteins
title Identification and characterization of a mouse cell mutant defective in the intracellular transport of glycoproteins
title_full Identification and characterization of a mouse cell mutant defective in the intracellular transport of glycoproteins
title_fullStr Identification and characterization of a mouse cell mutant defective in the intracellular transport of glycoproteins
title_full_unstemmed Identification and characterization of a mouse cell mutant defective in the intracellular transport of glycoproteins
title_short Identification and characterization of a mouse cell mutant defective in the intracellular transport of glycoproteins
title_sort identification and characterization of a mouse cell mutant defective in the intracellular transport of glycoproteins
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114779/
https://www.ncbi.nlm.nih.gov/pubmed/3040769