Abstract
The nuclear envelope (NE) of eukaryotic cells has a highly structural architecture, comprising double lipid-bilayer membranes, nuclear pore complexes, and an underlying nuclear lamina network. The NE structure is held in place through the membrane-bound LINC (linker of nucleoskeleton and cytoskeleton) complex, spanning the inner and outer nuclear membranes. The NE functions as a barrier between the nucleus and cytoplasm and as a transverse scaffold for various cellular processes. Epstein–Barr virus (EBV) is a human pathogen that infects most of the world’s population and is associated with several well-known malignancies. Within the nucleus, the replicated viral DNA is packaged into capsids, which subsequently egress from the nucleus into the cytoplasm for tegumentation and final envelopment. There is increasing evidence that viral lytic gene expression or replication contributes to the pathogenesis of EBV. Various EBV lytic proteins regulate and modulate the nuclear envelope structure in different ways, especially the viral BGLF4 kinase and the nuclear egress complex BFRF1/BFRF2. From the aspects of nuclear membrane structure, viral components, and fundamental nucleocytoplasmic transport controls, this review summarizes our findings and recently updated information on NE structure modification and NE-related cellular processes mediated by EBV.
Highlights
Our and others’ studies demonstrated that at least three virus-encoded proteins, including BGLF4 protein kinase and nuclear egress complex BFRF1/BFLF2, modify the nuclear envelope (NE) structure to facilitate the nucleocytoplasmic transport of nucleocapsids
We previously demonstrated that the expression of BGLF4 alone efficiently modulates chromatin structure and cytoskeleton arrangement, very similar to CDK1-induced promitotic events [57]
In addition to the endosomal sorting complex required for transport (ESCRT) components, we further demonstrated that the membrane modulating functions of BFRF1 are regulated by ubiquitination [119]
Summary
The nucleus is surrounded by an envelope composed of the inner and outer nuclear membranes, the perinuclear space between the membranes, and the underlying nuclear lamina network (Figure 1A) These three-layer structures are held in place by the nuclear pore complex (NPC), which functions as a transport gatekeeper for macromolecules trafficking in or out of the nucleus. The integrity of the envelope provides the structural support for nuclear morphology and functions as a platform for coordinating several cellular processes, including DNA repair, cell signaling, migration, and gene expression. With chemical stimulations or reactivation signals, the viral transactivator Zta or Rta. Viruses 2021, 13, 702 the terminal repeats and maintained as an episomal form in the latently infected cells. Such regulation could occur in as little as 30 min to activate gene transcription in response to challenge by various pathogens
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