Alex de Marco, Hans-Georg Kräusslich (auth.), Eric O. Freed's Advances in HIV-1 Assembly and Release PDF

By Alex de Marco, Hans-Georg Kräusslich (auth.), Eric O. Freed (eds.)

ISBN-10: 146147728X

ISBN-13: 9781461477280

ISBN-10: 1461477298

ISBN-13: 9781461477297

​Over the prior decade, huge, immense development has been made in realizing the past due occasions within the HIV replication cycle. This has been made attainable by way of significant advances in phone biology, virology, and structural biology. the sphere maintains to maneuver ahead swiftly, with vital new discoveries being stated regularly. The influence of this growth throughout a huge spectrum of biomedical learn has been enormous. the rise in simple wisdom within the parts of HIV meeting, liberate, and maturation has been observed by means of new percentages for healing intervention.The paintings contains subject matters in terms of uncomplicated molecular biology, mobile biology, and structural biology of HIV meeting, coupled with extra utilized principles of the way this uncomplicated details can tell the sector of antiretroviral examine. The booklet covers all significant issues bearing on the overdue levels of HIV replication, with leaders in each one sector recruited to give a contribution chapters of their parts of craftsmanship . the themes might be sufficiently targeted to permit authors the chance to hide the newest advancements in detail.​

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Additional info for Advances in HIV-1 Assembly and Release

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This can be driven through recruitment of ESCRT-0 (or equivalent proteins), -I and -II or by the ESCRT-associated protein AIP1/ALIX [141]. A number of enveloped viruses that use the ESCRT machinery to effect their release from cells have developed molecular mimics to drive ESCRT recruitment [143]. For HIV and related viruses, the p6 domain of Gag contains a so-called “late domain” that is required for virus scission and release [144, 145]. One late domain signal is a PTAP motif that mimics the PSAP motif in the ESCRT-0 protein Hrs to bind the Tsg101 component of ESCRT-I [10–13].

When expressed in polarised epithelial cells, HIV Env is sorted to the baso-lateral domain through the activity of its GYxxØ Cellular Trafficking Mechanisms in the Assembly and Release of HIV 37 motif, and can direct polarised VLP budding from this domain [126, 127]. Whether this activity has relevance for directing virus assembly in polarised T cells, MDM or dendritic cells remains unclear [128]. Rather than being directly targeted to the cell surface, Env has been suggested to traffic through CTLA-4-containing secretory granules, which might allow Env delivery to the PM to be regulated [129].

Nevertheless, a common thread seems to be a link to activation of the viral protease activity. Clathrin may thus provide spatial constraints that regulate protease activity and thereby influence particle maturation and infectivity. Release of Assembled HIV Particles The interaction of viral constituents with cellular trafficking machineries is crucial for ensuring that the components required to form infectious particles are collected together at the same time in the same cellular membrane domains.

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Advances in HIV-1 Assembly and Release by Alex de Marco, Hans-Georg Kräusslich (auth.), Eric O. Freed (eds.)

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