Abstract
Viruses are obligate parasites that rely on host cellular factors to replicate and spread. The endosomal sorting complexes required for transport (ESCRT) system, which is classically associated with sorting and downgrading surface proteins, is one of the host machineries hijacked by viruses across diverse families. Knowledge gained from research into ESCRT and viruses has, in turn, greatly advanced our understanding of many other cellular functions in which the ESCRT pathway is involved, e.g., cytokinesis. This review highlights the interplay between the ESCRT pathway and the viral factors of enveloped viruses with a special emphasis on retroviruses.
Highlights
[49], which arrives after recruitring of AAA-ATPase VPS4 [49], which arrives after endosomal sorting complexes required for transport (ESCRT)-III recruitment
The recruitment of ALIX during HIV-1 budding shows a dynamic burst once Gag multimerisation is completed [168], analogous to the late ESCRT acting components and unlike the progressive recruitment shown by TSG101 (3–5 min)
Learning how the ESCRT system is hijacked by viruses has greatly advanced our knowledge in understanding its normal cellular functions including cytokinesis and nuclear envelope sealing
Summary
The viral protein motifs involved acting at this period of assembly and budding were termed “late domains” (L domains). Identification of these critical regions spurred investigation into finding their cellular binding partners. Dominant negative versions of VPS4, an AAA-ATPase required for formation of multivesicular bodies (MVB) [10], were shown to block virus budding [5]. Together, these studies revolutionised our understanding of how HIV hijacks the host endosomal trafficking pathway to bud away from infected cells.
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