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Is there a role for actin in virus budding?

Electrophoretic data from both sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE) and acid-urea gels reveal a protein in purified murine mammary tumor virus (MuMTV) which co-migrates with purified chick skeletal muscle actin. 125I-labeling of intact and disrupted virus preparations shows that the...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1977
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109946/
https://www.ncbi.nlm.nih.gov/pubmed/233748
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description Electrophoretic data from both sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE) and acid-urea gels reveal a protein in purified murine mammary tumor virus (MuMTV) which co-migrates with purified chick skeletal muscle actin. 125I-labeling of intact and disrupted virus preparations shows that the actin-like protein is not artifactually adsorbed to the outside of virions during isolation. Quantitative SDS- PAGE and examination of negatively stained preparations show that the actin cannot be accounted for by a contaminating population of virus- free vesicles. The ultrastructure of mammary epithelial cells and of Rous sarcoma virus-transformed chick embryo fibroblasts shows that virus extrusion is associated with filament-containing cellular processes. In particular, MuMTV is released from the ends of long microvilli which contain a bundle of 6-8-nm microfilaments and share other structural features with intestinal microvilli. We suggest that virus nucleoids require an interaction with host cell contractile proteins for their extrusion from the cell.
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spelling pubmed-21099462008-05-01 Is there a role for actin in virus budding? J Cell Biol Articles Electrophoretic data from both sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE) and acid-urea gels reveal a protein in purified murine mammary tumor virus (MuMTV) which co-migrates with purified chick skeletal muscle actin. 125I-labeling of intact and disrupted virus preparations shows that the actin-like protein is not artifactually adsorbed to the outside of virions during isolation. Quantitative SDS- PAGE and examination of negatively stained preparations show that the actin cannot be accounted for by a contaminating population of virus- free vesicles. The ultrastructure of mammary epithelial cells and of Rous sarcoma virus-transformed chick embryo fibroblasts shows that virus extrusion is associated with filament-containing cellular processes. In particular, MuMTV is released from the ends of long microvilli which contain a bundle of 6-8-nm microfilaments and share other structural features with intestinal microvilli. We suggest that virus nucleoids require an interaction with host cell contractile proteins for their extrusion from the cell. The Rockefeller University Press 1977-11-01 /pmc/articles/PMC2109946/ /pubmed/233748 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
Is there a role for actin in virus budding?
title Is there a role for actin in virus budding?
title_full Is there a role for actin in virus budding?
title_fullStr Is there a role for actin in virus budding?
title_full_unstemmed Is there a role for actin in virus budding?
title_short Is there a role for actin in virus budding?
title_sort is there a role for actin in virus budding?
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109946/
https://www.ncbi.nlm.nih.gov/pubmed/233748