The Role of ND10 Nuclear Bodies in Herpesvirus Infection: A Frenemy for the Virus?

Fada, Behdokht Jan; Reward, Eleazar E.; Gu, Howard H.

doi:10.3390/v13020239

Cited by 8 publications

(6 citation statements)

References 183 publications

(175 reference statements)

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“…The loss of the ICP0 N-terminus showed a moderate reduction of viral yield and a delayed expression of the true late protein gC, indicating a role of the ICP0 N-terminus in HSV-1 infection. ND10 has been reported to have both positive and negative effects on HSV-1 and other herpes infections [ 27 , 52 ]. It remains unclear whether the differential PML ubiquitination catalyzed by ICP0 affects the interaction between ICP0 and other ND10 components besides dispersing the ND10 structure and, more importantly, whether there are ND10 components differentially ubiquitinated by ICP0 but which are not degraded via proteasomes.…”

Section: Discussionmentioning

confidence: 99%

“…Upon HSV-1 entry, ND10 components converge to the incoming DNA to restrict viral expression [ 7 , 24 , 25 ]. ICP0 E3-mediated PML and Sp100 degradation help to disperse ND10 components and thereby release the DNA repression imposed by ND10 [ 26 , 27 ]. The siRNA knockdown of PML and Sp100 enhances the growth of HSV-1 in the absence of ICP0 [ 28 , 29 ].…”

Section: Introductionmentioning

confidence: 99%

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A Novel Recognition by the E3 Ubiquitin Ligase of HSV-1 ICP0 Enhances the Degradation of PML Isoform I to Prevent ND10 Reformation in Late Infection

Fada

Guha

Zheng

et al. 2023

Viruses

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Upon viral entry, components of ND10 nuclear bodies converge with incoming DNA to repress viral expression. The infected cell protein 0 (ICP0) of herpes simplex virus 1 (HSV-1) contains a RING-type E3 ubiquitin ligase that targets the ND10 organizer, PML, for proteasomal degradation. Consequently, ND10 components are dispersed and viral genes are activated. Previously, we reported that ICP0 E3 differentiates two similar substrates, PML isoforms I and II, and demonstrated that SUMO-interaction has profound regulatory effects on PML II degradation. In the present study, we investigated elements that regulate the PML I degradation and found that: (i) two regions of ICP0 flanking the RING redundantly facilitate the degradation of PML I; (ii) downstream of the RING, the SUMO-interaction motif located at residues 362–364 (SIM362–364) targets the SUMOylated PML I in the same manner as that of PML II; (iii) upstream of the RING, the N-terminal residues 1–83 mediate PML I degradation regardless of its SUMOylation status or subcellular localization; (iv) the reposition of residues 1–83 to downstream of the RING does not affect its function in PML I degradation; and (v) the deletion of 1–83 allows the resurgence of PML I and reformation of ND10-like structures late in HSV-1 infection. Taken together, we identified a novel substrate recognition specific for PML I, by which ICP0 E3 enforces a continuous PML I degradation throughout the infection to prevent the ND10 reformation.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A Novel Recognition by the E3 Ubiquitin Ligase of HSV-1 ICP0 Enhances the Degradation of PML Isoform I to Prevent ND10 Reformation in Late Infection

Fada

Guha

Zheng

et al. 2023

Viruses

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“…Meanwhile, several studies have indicated that some PML NB components can be advantageous for herpesvirus infection and the establishment of latent infection. These observations suggest that PML NBs may play both pro-viral and antiviral roles, reviewed in [ 98 ].…”

Section: The Structure Composition and Function Of Pml Nbsmentioning

confidence: 99%

The interactions between PML nuclear bodies and small and medium size DNA viruses

Ryabchenko

Šroller

Horníková

et al. 2023

Virol J

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Promyelocytic leukemia nuclear bodies (PM NBs), often referred to as membraneless organelles, are dynamic macromolecular protein complexes composed of a PML protein core and other transient or permanent components. PML NBs have been shown to play a role in a wide variety of cellular processes. This review describes in detail the diverse and complex interactions between small and medium size DNA viruses and PML NBs that have been described to date. The PML NB components that interact with small and medium size DNA viruses include PML protein isoforms, ATRX/Daxx, Sp100, Sp110, HP1, and p53, among others. Interaction between viruses and components of these NBs can result in different outcomes, such as influencing viral genome expression and/or replication or impacting IFN-mediated or apoptotic cell responses to viral infection. We discuss how PML NB components abrogate the ability of adenoviruses or Hepatitis B virus to transcribe and/or replicate their genomes and how papillomaviruses use PML NBs and their components to promote their propagation. Interactions between polyomaviruses and PML NBs that are poorly understood but nevertheless suggest that the NBs can serve as scaffolds for viral replication or assembly are also presented. Furthermore, complex interactions between the HBx protein of hepadnaviruses and several PML NBs-associated proteins are also described. Finally, current but scarce information regarding the interactions of VP3/apoptin of the avian anellovirus with PML NBs is provided. Despite the considerable number of studies that have investigated the functions of the PML NBs in the context of viral infection, gaps in our understanding of the fine interactions between viruses and the very dynamic PML NBs remain. The complexity of the bodies is undoubtedly a great challenge that needs to be further addressed.

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“…Viruses may trigger the degradation of heterochromatin components, such as Smc5/6, which is targeted by HBV, or components of PML bodies, which provide a favorable environment for heterochromatin formation (139,140). This can, for example, be PML itself or SP100, which are targeted by HSV-1 (141), or ATRX/DAXX, targeted by adenovirus (139).…”

Section: Viruses Drive Global Genome Opening By Switching or Tuning S...mentioning

confidence: 99%

ProA and ProB repeat sequences shape genome organization, and enhancers open domains

Bonnet,

Hulo,

Mourad

et al. 2023

Preprint

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SUMMARYThere is a growing awareness that repeat sequences (RepSeq) - the main constituents of the human genome - are also prime players in its organization. Here we propose that the genome should be envisioned as a supersystem with three main subsystems, each composed of functionally redundant, cooperating elements. We define herein ProA and ProB RepSeqs as sequences that promote either the A/euchromatin or the B/heterochromatin compartment. ProA and ProB RepSeqs shape A/B partitioning, such that the relative proportions of ProA and ProB RepSeqs determine the propensity of a chromosome segment to adopt either an A or a B configuration. In human, core ProA RepSeqs are essentially made of Alu elements, whereas core ProB RepSeqs consist of young L1 and some Endogenous Retroviruses (ERVs) as well as a panel of AT-rich microsatellites and pericentromeric and telomeric satellites. Additionally, RepSeqs with more indefinite character and, importantly, their derivatives known as “transcriptional enhancers”, can shift between ProA and ProB functions and thus act to open or close specific chromatin domains depending on the cellular context. In this framework, genes and their promoters appear as a special class of RepSeqs that, in their active, transcribed state, reinforce the openness of their surroundings. Molecular mechanisms involve cooperativity between ProB elements, presumably underpinned by the condensate-like properties of heterochromatin, which ProA elements oppose in several ways. We provide strong arguments that altered CpG methylation patterns in cancer including a marked loss in the B compartment, result primarily from a global imbalance in the process of CpG methylation and its erasure. Our results suggest that the resulting altered methylation and impaired function of ProB RepSeqs globally weaken the B compartment, rendering it more plastic, which in turn may confer fate plasticity to the cancer cell.

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The Role of ND10 Nuclear Bodies in Herpesvirus Infection: A Frenemy for the Virus?

Cited by 8 publications

References 183 publications

A Novel Recognition by the E3 Ubiquitin Ligase of HSV-1 ICP0 Enhances the Degradation of PML Isoform I to Prevent ND10 Reformation in Late Infection

A Novel Recognition by the E3 Ubiquitin Ligase of HSV-1 ICP0 Enhances the Degradation of PML Isoform I to Prevent ND10 Reformation in Late Infection

The interactions between PML nuclear bodies and small and medium size DNA viruses

ProA and ProB repeat sequences shape genome organization, and enhancers open domains

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