The Mechanism of Budding of Retroviruses from Cell Membranes
Author(s) -
Andrew Pincetic,
Jonathan Leis
Publication year - 2009
Publication title -
advances in virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.956
H-Index - 25
eISSN - 1687-8647
pISSN - 1687-8639
DOI - 10.1155/2009/623969
Subject(s) - escrt , budding , biogenesis , mechanism (biology) , microbiology and biotechnology , biology , virology , tsg101 , ubiquitin , virus , viral envelope , endogenous retrovirus , chemistry , endosome , genetics , microvesicles , genome , intracellular , gene , philosophy , epistemology , microrna
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 adopt parallel budding pathways by recruiting different host factors from common cellular machinery for particle release.
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