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 Ga...

Full description

Bibliographic Details
Main Authors: Andrew Pincetic, Jonathan Leis
Format: Article
Language:English
Published: Hindawi Limited 2009-01-01
Series:Advances in Virology
Online Access:http://dx.doi.org/10.1155/2009/623969
id doaj-54f38cfd24074f478ead2730f7541d3e
record_format Article
spelling doaj-54f38cfd24074f478ead2730f7541d3e2021-07-02T07:18:40ZengHindawi LimitedAdvances in Virology1687-86391687-86472009-01-01200910.1155/2009/623969623969The Mechanism of Budding of Retroviruses from Cell MembranesAndrew Pincetic0Jonathan Leis1Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USADepartment of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USARetroviruses 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.http://dx.doi.org/10.1155/2009/623969
collection DOAJ
language English
format Article
sources DOAJ
author Andrew Pincetic
Jonathan Leis
spellingShingle Andrew Pincetic
Jonathan Leis
The Mechanism of Budding of Retroviruses from Cell Membranes
Advances in Virology
author_facet Andrew Pincetic
Jonathan Leis
author_sort Andrew Pincetic
title The Mechanism of Budding of Retroviruses from Cell Membranes
title_short 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_sort mechanism of budding of retroviruses from cell membranes
publisher Hindawi Limited
series Advances in Virology
issn 1687-8639
1687-8647
publishDate 2009-01-01
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.
url http://dx.doi.org/10.1155/2009/623969
work_keys_str_mv AT andrewpincetic themechanismofbuddingofretrovirusesfromcellmembranes
AT jonathanleis themechanismofbuddingofretrovirusesfromcellmembranes
AT andrewpincetic mechanismofbuddingofretrovirusesfromcellmembranes
AT jonathanleis mechanismofbuddingofretrovirusesfromcellmembranes
_version_ 1721336246465200128