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The Mechanism of Budding of Retroviruses from Cell Membranes

Retroviruses have evolved a mechanism for the release of particles from the cell membrane that appropriates cellular protein complexes, referred to as ESCRT-I, -II, -III, normally involved in the biogenesis of multivesicular bodies. Three different classes of late assembly (L) domains encoded in Gag...

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Detalles Bibliográficos
Autores principales: Pincetic, Andrew, Leis, Jonathan
Formato: Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2768365/
https://www.ncbi.nlm.nih.gov/pubmed/19865606
http://dx.doi.org/10.1155/2009/623969
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author Pincetic, Andrew
Leis, Jonathan
author_facet Pincetic, Andrew
Leis, Jonathan
author_sort Pincetic, Andrew
collection PubMed
description Retroviruses have evolved a mechanism for the release of particles from the cell membrane that appropriates cellular protein complexes, referred to as ESCRT-I, -II, -III, normally involved in the biogenesis of multivesicular bodies. Three different classes of late assembly (L) domains encoded in Gag, with core sequences of PPXY, PTAP, and YPXL, recruit different components of the ESCRT machinery to form a budding complex for virus release. Here, we highlight recent progress in identifying the role of different ESCRT complexes in facilitating budding, ubiquitination, and membrane targeting of avian sarcoma and leukosis virus (ASLV) and human immunodeficiency virus, type 1 (HIV-1). These findings show that retroviruses may adopt parallel budding pathways by recruiting different host factors from common cellular machinery for particle release.
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spelling pubmed-27683652009-10-27 The Mechanism of Budding of Retroviruses from Cell Membranes Pincetic, Andrew Leis, Jonathan Adv Virol Review Article Retroviruses have evolved a mechanism for the release of particles from the cell membrane that appropriates cellular protein complexes, referred to as ESCRT-I, -II, -III, normally involved in the biogenesis of multivesicular bodies. Three different classes of late assembly (L) domains encoded in Gag, with core sequences of PPXY, PTAP, and YPXL, recruit different components of the ESCRT machinery to form a budding complex for virus release. Here, we highlight recent progress in identifying the role of different ESCRT complexes in facilitating budding, ubiquitination, and membrane targeting of avian sarcoma and leukosis virus (ASLV) and human immunodeficiency virus, type 1 (HIV-1). These findings show that retroviruses may adopt parallel budding pathways by recruiting different host factors from common cellular machinery for particle release. Hindawi Publishing Corporation 2009 2009-03-05 /pmc/articles/PMC2768365/ /pubmed/19865606 http://dx.doi.org/10.1155/2009/623969 Text en Copyright © 2009 A. Pincetic and J. Leis. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Pincetic, Andrew
Leis, Jonathan
The Mechanism of Budding of Retroviruses from Cell Membranes
title The Mechanism of Budding of Retroviruses from Cell Membranes
title_full The Mechanism of Budding of Retroviruses from Cell Membranes
title_fullStr The Mechanism of Budding of Retroviruses from Cell Membranes
title_full_unstemmed The Mechanism of Budding of Retroviruses from Cell Membranes
title_short The Mechanism of Budding of Retroviruses from Cell Membranes
title_sort mechanism of budding of retroviruses from cell membranes
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2768365/
https://www.ncbi.nlm.nih.gov/pubmed/19865606
http://dx.doi.org/10.1155/2009/623969
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