Confined no more: Viral mechanisms of nuclear entry and egress

Molenberghs, Freya; Bogers, Johannes; Vos, Winnok H. De

doi:10.1016/j.biocel.2020.105875

Cited by 8 publications

(7 citation statements)

References 131 publications

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“…Thus, the core NEC proteins may activate and optimize the mitotic NEBD to use this mechanism in a more specific and efficient way for herpesviral replication and hence, can rely on this less efficient mitotic NEBD when the functionality of the core NEC proteins is disturbed. Moreover, it is noteworthy to mention that in addition to herpesviruses, several other viruses have to overcome this physico-chemical barrier of NE to enter or exit the nucleus and, hence, remodel the NE, albeit in various ways [ 111 , 112 , 113 ]. For example, the simian virus 40 (SV40) restructures the NE by the activation of specific caspases resulting in a direct cleavage of lamins and lamin-associated proteins, consequently hijacking the apoptosis-specific mechanism to mediate NEBD, but without inducing the complete pathway of programmed cell death [ 113 ].…”

Section: Mutational Analysis Focusing On Specific Herpesviral Nec Fun...mentioning

confidence: 99%

“…Moreover, it is noteworthy to mention that in addition to herpesviruses, several other viruses have to overcome this physico-chemical barrier of NE to enter or exit the nucleus and, hence, remodel the NE, albeit in various ways [ 111 , 112 , 113 ]. For example, the simian virus 40 (SV40) restructures the NE by the activation of specific caspases resulting in a direct cleavage of lamins and lamin-associated proteins, consequently hijacking the apoptosis-specific mechanism to mediate NEBD, but without inducing the complete pathway of programmed cell death [ 113 ].…”

Section: Mutational Analysis Focusing On Specific Herpesviral Nec Fun...mentioning

confidence: 99%

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‘Come together’—The Regulatory Interaction of Herpesviral Nuclear Egress Proteins Comprises Both Essential and Accessory Functions

Häge

Marschall

2022

Cells

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Herpesviral nuclear egress is a fine-tuned regulatory process that defines the nucleocytoplasmic release of viral capsids. Nuclear capsids are unable to traverse via nuclear pores due to the fact of their large size; therefore, herpesviruses evolved to develop a vesicular transport pathway mediating the transition across the two leaflets of the nuclear membrane. The entire process involves a number of regulatory proteins, which support the local distortion of the nuclear envelope. In the case of the prototype species of β-Herpesvirinae, the human cytomegalovirus (HCMV), the nuclear egress complex (NEC) is determined by the core proteins pUL50 and pUL53 that oligomerize, form capsid docking lattices and mediate multicomponent assembly with NEC-associated viral and cellular proteins. The NEC-binding principle is based on the hook-into-groove interaction through an N-terminal hook-like pUL53 protrusion that embraces an α-helical pUL50 binding groove. Thus far, the function and characteristics of herpesviral core NECs have been well studied and point to the groove proteins, such as pUL50, as the multi-interacting, major determinants of NEC formation and egress. This review provides closer insight into (i) sequence and structure conservation of herpesviral core NEC proteins, (ii) experimentation on cross-viral core NEC interactions, (iii) the essential functional roles of hook and groove proteins for viral replication, (iv) an establishment of assay systems for NEC-directed antiviral research and (v) the validation of NEC as putative antiviral drug targets. Finally, this article provides new insights into the conservation, function and antiviral targeting of herpesviral core NEC proteins and, into the complex regulatory role of hook and groove proteins during the assembly, egress and maturation of infectious virus.

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Section: Mutational Analysis Focusing On Specific Herpesviral Nec Fun...mentioning

confidence: 99%

Section: Mutational Analysis Focusing On Specific Herpesviral Nec Fun...mentioning

confidence: 99%

‘Come together’—The Regulatory Interaction of Herpesviral Nuclear Egress Proteins Comprises Both Essential and Accessory Functions

Häge

Marschall

2022

Cells

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“…However, studies reported that there are mechanisms with which no virus entry has so far connected. These incorporate the flotillin pathway, the ADP-ribosylation factor 6 (Arf6) pathway, the glycosylphosphotidylinositol-anchored protein (GPI-AP) enriched compartments (GEEC) pathway, and the interleukin (IL-2) pathway [ 47 ]. The respiratory viruses' transmission mode, target cell, receptors of host cells, entry pathways, virus and host cell expressed proteins, pathogenesis, and symptoms are disclosed in Table 2 .…”

Section: Transmission Mode and Cell Invasion Pathways Of The Respiratory Virusmentioning

confidence: 99%

Human respiratory viral infections: Current status and future prospects of nanotechnology-based approaches for prophylaxis and treatment

Dawre

Maru

2021

Life Sciences

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“…Not surprisingly, many links have long been noticed between the replication cycle of retroelements and NPCs (Figure 2A). Indeed, the NPC has been early described as the main route for the nuclear export of viral mRNAs and the nuclear import of pre-integration complexes (PICs) (reviewed in (Molenberghs et al, 2020)). The role played by the NPCs and other cellular factors in nuclear import of HIV-1 PIC has been particularly well studied (reviewed in (Bhargava et al, 2018)).…”

Section: Local Chromatin Features and 3d Genome Organization May Influence Ty Integration Site Selectionmentioning

confidence: 99%

Light and shadow on the mechanisms of integration site selection in yeast Ty retrotransposon families

Bonnet

Lesage

2021

Curr Genet

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Transposable elements are ubiquitous in genomes. Their successful expansion depends in part on their sites of integration in their host genome. In Saccharomyces cerevisiae, evolution has selected various strategies to target the five Ty LTR-retrotransposon families into gene-poor regions in a genome, where coding sequences occupy 70% of the DNA. The integration of Ty1/Ty2/Ty4 and Ty3 occurs upstream and at the transcription start site of the genes transcribed by RNA polymerase III, respectively. Ty5 has completely different integration site preferences, targeting heterochromatin regions. Here, we review the history that led to the identification of the cellular tethering factors that play a major role in anchoring Ty retrotransposons to their preferred sites. We also question the involvement of additional factors in the fine-tuning of the integration site selection, with several studies converging towards an importance of the structure and organization of the chromatin.

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Confined no more: Viral mechanisms of nuclear entry and egress

Cited by 8 publications

References 131 publications

‘Come together’—The Regulatory Interaction of Herpesviral Nuclear Egress Proteins Comprises Both Essential and Accessory Functions

‘Come together’—The Regulatory Interaction of Herpesviral Nuclear Egress Proteins Comprises Both Essential and Accessory Functions

Human respiratory viral infections: Current status and future prospects of nanotechnology-based approaches for prophylaxis and treatment

Light and shadow on the mechanisms of integration site selection in yeast Ty retrotransposon families

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