Essential Ingredients for HIV-1 Budding
نویسندگان
چکیده
منابع مشابه
Tsg101 and the Vacuolar Protein Sorting Pathway Are Essential for HIV-1 Budding
Like other enveloped viruses, HIV-1 uses cellular machinery to bud from infected cells. We now show that Tsg101 protein, which functions in vacuolar protein sorting (Vps), is required for HIV-1 budding. The UEV domain of Tsg101 binds to an essential tetrapeptide (PTAP) motif within the p6 domain of the structural Gag protein and also to ubiquitin. Depletion of cellular Tsg101 by small interferi...
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HIV-1 Gag engages components of the ESCRT (endosomal sorting complex required for transport) pathway via so-called L (late-assembly) domains to promote virus budding. Specifically, the PTAP (Pro-Thr-Ala-Pro)-type primary L domain of HIV-1 recruits ESCRT-I by binding to Tsg101 (tumour susceptibility gene 101), and an auxiliary LYPX(n)L (Leu-Tyr-Pro-Xaa(n)-Leu)-type L domain recruits the ESCRT-II...
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A defining property of retroviruses is their ability to assemble into particles that can leave producer cells and spread infection to susceptible cells and hosts. Virion morphogenesis can be divided into three stages: assembly, wherein the virion is created and essential components are packaged; budding, wherein the virion crosses the plasma membrane and obtains its lipid envelope; and maturati...
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Within the last years, ambitions towards the definition of common interfaces and the development of open frameworks have been increasing the efficiency of research on WCET analysis. The Annotation Language Challenge for WCET analysis has been proposed with the intention to underline the importance of such common interfaces. Within this paper we present a list of essential ingredients for a comm...
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Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AM...
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ژورنال
عنوان ژورنال: Cell Host & Microbe
سال: 2011
ISSN: 1931-3128
DOI: 10.1016/j.chom.2011.03.005