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...
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| Format: | Article |
| Language: | English |
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Wiley
2009-01-01
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| Series: | Advances in Virology |
| Online Access: | http://dx.doi.org/10.1155/2009/623969 |
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| _version_ | 1850226437232001024 |
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| author | Andrew Pincetic Jonathan Leis |
| author_facet | Andrew Pincetic Jonathan Leis |
| author_sort | Andrew Pincetic |
| collection | DOAJ |
| 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. |
| format | Article |
| id | doaj-art-54f38cfd24074f478ead2730f7541d3e |
| institution | OA Journals |
| issn | 1687-8639 1687-8647 |
| language | English |
| publishDate | 2009-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Advances in Virology |
| spelling | doaj-art-54f38cfd24074f478ead2730f7541d3e2025-08-20T02:05:04ZengWileyAdvances 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 |
| spellingShingle | Andrew Pincetic Jonathan Leis The Mechanism of Budding of Retroviruses from Cell Membranes Advances in Virology |
| 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 |
| url | http://dx.doi.org/10.1155/2009/623969 |
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