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Updated: Sep 21, 2026

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
Published on: November 4, 2018
Interaction of EBV latent origin of replication with the nuclear matrix: identification of S/MAR sequences and
Giulia Mearini1, Silvia Chichiarelli, Michele Zampieri
1Department of Public Health Sciences, University La Sapienza, Rome, Italy. giulia.mearini@hpi.uni-hamburg.de <giulia.mearini@hpi.uni-hamburg.de>
Abstract:
During latency, Epstein Barr virus (EBV) genome, as an episome, is attached to the nuclear matrix (NM) via the latent origin of replication ori P. Within this element, we have found that a region, 580 bp long, encompassing the replicator DS element, shows the strongest affinity for the NM. In addition, by cross-linking with cis-diamminedichloroplatinum, we have identified two NM proteins with an apparent molecular weight of 85 and 60 kDa that, with high affinity and specificity, bind ori P. These proteins are not induced by EBV infection, but their interaction with ori P is lost upon induction of EBV lytic cycle. These data strongly suggest that the binding of ori P to specific components of the NM is required for EBV latent replication.
Insights
Epstein Barr virus (EBV) DNA attaches to the nuclear matrix during latency via the ori P region. Specific nuclear matrix proteins bind ori P, essential for EBV
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Epstein Barr virus (EBV) establishes lifelong latency in humans.
- During latency, the EBV genome exists as an episome attached to the host cell's nuclear matrix (NM).
- Attachment to the NM is mediated by the latent origin of replication, ori P.
Purpose of the Study:
- To investigate the specific EBV DNA sequences and nuclear matrix proteins involved in EBV genome attachment.
- To understand the role of this interaction in EBV latent replication.
Main Methods:
- Used a 580 bp DNA fragment from the EBV ori P region to identify binding sites to the nuclear matrix.
- Employed cis-diamminedichloroplatinum cross-linking to identify interacting nuclear matrix proteins.
- Analyzed protein-DNA interactions and their modulation during EBV lytic cycle induction.
Main Results:
- A 580 bp region within EBV's ori P, including the DS element, demonstrated the highest affinity for the nuclear matrix.
- Two nuclear matrix proteins (85 and 60 kDa) were identified that bind specifically to ori P.
- These proteins are constitutively present and their interaction with ori P is disrupted during the EBV lytic cycle.
Conclusions:
- Specific binding of EBV's ori P to nuclear matrix proteins is crucial for maintaining EBV episomal attachment.
- This interaction is essential for Epstein Barr virus latent replication.
- The identified proteins and their interaction represent a potential target for controlling EBV latency.
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