Abrogating ALIX Interactions Results in Stuttering of the ESCRT Machinery

Gupta, Shilpa; Bendjennat, Mourad; Saffarian, Saveez

doi:10.3390/v12091032

Cited by 11 publications

(9 citation statements)

References 77 publications

(118 reference statements)

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“…For example, ALIX recruitment via a YPXL domain is not essential in HIV-1 budding if a PTAP-TSG101 interaction is present. However, a recent study showed that ALIX is required for the efficient engagement of CHMP4B and VPS4 [ 80 ]. Multiple late domains may also play distinct roles at different stages of the assembly of the same virus.…”

Section: Viral Factors Involved In Entry To the Escrt Pathwaymentioning

confidence: 99%

The Interplay between ESCRT and Viral Factors in the Enveloped Virus Life Cycle

Meng

Lever

2021

Viruses

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Viruses are obligate parasites that rely on host cellular factors to replicate and spread. The endosomal sorting complex 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.

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Section: Viral Factors Involved In Entry To the Escrt Pathwaymentioning

confidence: 99%

The Interplay between ESCRT and Viral Factors in the Enveloped Virus Life Cycle

Meng

Lever

2021

Viruses

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“…ALIX is also an essential component of this process and exhibits the same localization pattern, as does ESCRT-I [47]. By binding to a spatially separated L-domain from that of ESCRT-I, ALIX can localize to the budding neck lumen and recruit ESCRT-III directly by virtue of its p6-binding V domain and CHMP4B-binding Bro1 domain, respectively [47][48][49]. Evidence of these structures have been captured in relevant cell types as well as in vitro [44,50,51].…”

Section: A Hexagonal Assembly Of Hiv-1 Gag Drives Particle Maturation and Escrt Recruitmentmentioning

confidence: 99%

When in Need of an ESCRT: The Nature of Virus Assembly Sites Suggests Mechanistic Parallels between Nuclear Virus Egress and Retroviral Budding

Rose

2021

Viruses

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The proper assembly and dissemination of progeny virions is a fundamental step in virus replication. As a whole, viruses have evolved a myriad of strategies to exploit cellular compartments and mechanisms to ensure a successful round of infection. For enveloped viruses such as retroviruses and herpesviruses, acquisition and incorporation of cellular membrane is an essential process during the formation of infectious viral particles. To do this, these viruses have evolved to hijack the host Endosomal Sorting Complexes Required for Transport (ESCRT-I, -II, and -III) to coordinate the sculpting of cellular membrane at virus assembly and dissemination sites, in seemingly different, yet fundamentally similar ways. For instance, at the plasma membrane, ESCRT-I recruitment is essential for HIV-1 assembly and budding, while it is dispensable for the release of HSV-1. Further, HSV-1 was shown to recruit ESCRT-III for nuclear particle assembly and egress, a process not used by retroviruses during replication. Although the cooption of ESCRTs occurs in two separate subcellular compartments and at two distinct steps for these viral lifecycles, the role fulfilled by ESCRTs at these sites appears to be conserved. This review discusses recent findings that shed some light on the potential parallels between retroviral budding and nuclear egress and proposes a model where HSV-1 nuclear egress may occur through an ESCRT-dependent mechanism.

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“…Each data point represents a cell (n = 8 cells for ALIX, and n = 12 cells for FL EAP45) processed with the pipeline illustrated in, B. Welch's two sample t test was used to compare the colocalisation results from ALIX and Gag, to those of FL EAP45 and Gag subsequent recruitment of other ESCRT components. 14,17 We transfected piGFP into an mCherry-ALIX expressing HeLa cell line. 35 One day post-transfection, the cells were fixed and examined using TIRF microscopy.…”

Section: Spatial Co-occurrence Analysis Using Widefield Tirf Microscopymentioning

confidence: 99%

“…The assembly of Gag particles at the cell membrane during HIV budding has been reported to occur within a time frame of $10 minutes, 11,47 and the dynamics of ESCRT protein recruitment by Gag particles have been reported for TSG101, 11,16 VPS4A, 5,12,15,17 some CHMP proteins of ESCRT-III 5,11 and ALIX, 14,17 with an association time at the membrane for different components varying from as little as a few seconds up to 20 minutes. To further validate the observed association between Gag and EAP45, and to analyse its dynamics, we used TIRF microscopy in live HeLa cells to visualise the spatiotemporal relationship between GFP-Gag and SNAP-FL EAP45 at the plasma membrane.…”

Section: Single Particle Tracking In Live Hela Cells Shows Transient Colocalisation Of Gag and Eap45mentioning

confidence: 99%

“…14 ESCRT-III components are recruited to the budding site and remain there for 3-5 minutes 11 with recent data indicating recurrent transient recruitment of CHMP4B and VPS4 until successful cleavage occurs. 5,17 Because of the transitory nature of these recruitments, the temporal co-occurrence between various components of ESCRT with Gag is very low, with only $1% to 4% of the total Gag at the plasma membrane detectably colocalised with an ESCRT component, as measured by direct stochastic optical reconstruction microscopy (dSTORM). 18 Extensive work has been carried out in elucidating the function of ESCRT-I and ESCRT-III in HIV budding and in other cellular processes, 19 however the role of ESCRT-II is still emerging.…”

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EAP45 association with budding HIV‐1: Kinetics and domain requirements

Meng

Ramirez

Scherer

et al. 2021

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A number of viruses including HIV use the ESCRT system to bud from the infected cell. We have previously confirmed biochemically that ESCRT-II is involved in this process in HIV-1 and have defined the molecular domains that are important for this.Here, using SNAP-tag fluorescent labelling and both fixed and live cell imaging we show that the ESCRT-II component EAP45 colocalises with the HIV protein Gag at the plasma membrane in a temporal and quantitative manner, similar to that previously shown for ALIX and Gag. We show evidence that a proportion of EAP45 may be packaged within virions, and we confirm the importance of the N terminus of EAP45 and specifically the H0 domain in this process. By contrast, the Glue domain of EAP45 is more critical for recruitment during cytokinesis, emphasising that viruses have ways of recruiting cellular components that may be distinct from those used by some cellular processes. This raises the prospect of selective interference with the pathway to inhibit viral function while leaving cellular functions relatively unperturbed.

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Abrogating ALIX Interactions Results in Stuttering of the ESCRT Machinery

Cited by 11 publications

References 77 publications

The Interplay between ESCRT and Viral Factors in the Enveloped Virus Life Cycle

The Interplay between ESCRT and Viral Factors in the Enveloped Virus Life Cycle

When in Need of an ESCRT: The Nature of Virus Assembly Sites Suggests Mechanistic Parallels between Nuclear Virus Egress and Retroviral Budding

EAP45 association with budding HIV‐1: Kinetics and domain requirements

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