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Dr. Chung-Pei Lee
School of Nursing, National Taipei University of Nursing and Health Sciences

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0 Nuclear Envelope
0 Epstein-Barr Virus
0 virus-host interactions
0 Nuclear egress
0 Virus maturation

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Review
Published: 18 April 2021 in Viruses
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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.

ACS Style

Chung-Pei Lee; Mei-Ru Chen. Conquering the Nuclear Envelope Barriers by EBV Lytic Replication. Viruses 2021, 13, 702 .

AMA Style

Chung-Pei Lee, Mei-Ru Chen. Conquering the Nuclear Envelope Barriers by EBV Lytic Replication. Viruses. 2021; 13 (4):702.

Chicago/Turabian Style

Chung-Pei Lee; Mei-Ru Chen. 2021. "Conquering the Nuclear Envelope Barriers by EBV Lytic Replication." Viruses 13, no. 4: 702.

Journal article
Published: 27 January 2021 in Antibiotics
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Lactoferrin (LF) is a multifunctional protein found in mammals, and it shows broad-spectrum antimicrobial activity. To improve the functional properties of specific probiotics in order to provide both the beneficial characteristics of lactic acid bacteria and the biological activity of LF, cDNAs of bovine LF (BLF), human LF (HLF), or porcine LF (PLF) were cloned into a nisin-inducible plasmid. These were then transformed into the selected eight probiotics, which are LF-resistant hosts. Expression of recombinant LFs (rLFs) was analyzed via SDS-PAGE and Western blot analysis. Although the selected host strains may not contain the nisRK genes (NisK, the sensor kinase; NisR, the regulator protein), the components of autoregulation, a low level of LFs expression can be successfully induced by using nisin within bacterial cells in a time-dependent manner in three engineered clones, including Lactobacillus delbrueckii/HLF, L. delbrueckii/BLF, and L. gasseri/BLF. Lactobacillus delbrueckii and Lactobacillus gasseri originate from yogurt and human milk, respectively, and both strains are functional probiotic strains. Therefore, we further compared the antibacterial activities of disrupted recombinant probiotic clones, conventional strains (host control), and vector control ones by using agar diffusion and broth inhibition analysis, and the expression of rLFs in the above three clones considerately improved their antibacterial efficacies against four important food-borne pathogens, namely, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis, and Salmonellaenterica. In conclusion, this study provides a simple strategy for the production of functional LFs (BLF and HLF) in both functional and LF-resistant hosts for applications in the field.

ACS Style

Zhen-Shu Liu; Chuen-Fu Lin; Chung-Pei Lee; Min-Chi Hsieh; Hung-Fu Lu; Ying-Fang Chen; Yu-We Ku; Po-Wen Chen. A Single Plasmid of Nisin-Controlled Bovine and Human Lactoferrin Expressing Elevated Antibacterial Activity of Lactoferrin-Resistant Probiotic Strains. Antibiotics 2021, 10, 120 .

AMA Style

Zhen-Shu Liu, Chuen-Fu Lin, Chung-Pei Lee, Min-Chi Hsieh, Hung-Fu Lu, Ying-Fang Chen, Yu-We Ku, Po-Wen Chen. A Single Plasmid of Nisin-Controlled Bovine and Human Lactoferrin Expressing Elevated Antibacterial Activity of Lactoferrin-Resistant Probiotic Strains. Antibiotics. 2021; 10 (2):120.

Chicago/Turabian Style

Zhen-Shu Liu; Chuen-Fu Lin; Chung-Pei Lee; Min-Chi Hsieh; Hung-Fu Lu; Ying-Fang Chen; Yu-We Ku; Po-Wen Chen. 2021. "A Single Plasmid of Nisin-Controlled Bovine and Human Lactoferrin Expressing Elevated Antibacterial Activity of Lactoferrin-Resistant Probiotic Strains." Antibiotics 10, no. 2: 120.

Journal article
Published: 11 March 2020 in Viruses
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Nuclear egress is a regulated process shared by α-, β- and γ-herpesviruses. The core nuclear egress complex (NEC) is composed of the membrane-anchored protein homologs of human cytomegalovirus (HCMV) pUL50, murine cytomegalovirus (MCMV) pM50, Epstein–Barr virus (EBV) BFRF1 or varicella zoster virus (VZV) Orf24, which interact with the autologous NEC partners pUL53, pM53, BFLF2 or Orf27, respectively. Their recruitment of additional proteins leads to the assembly of a multicomponent NEC, coordinately regulating viral nucleocytoplasmic capsid egress. Here, the functionality of VZV, HCMV, MCMV and EBV core NECs was investigated by coimmunoprecipitation and confocal imaging analyses. Furthermore, a recombinant MCMV, harboring a replacement of ORF M50 by UL50, was analyzed both in vitro and in vivo. In essence, core NEC interactions were strictly limited to autologous NEC pairs and only included one measurable nonautologous interaction between the homologs of HCMV and MCMV. A comparative analysis of MCMV-WT versus MCMV-UL50-infected murine fibroblasts revealed almost identical phenotypes on the levels of protein and genomic replication kinetics. In infected BALB/c mice, virus spread to lung and other organs was found comparable between these viruses, thus stating functional complementarity. In conclusion, our study underlines that herpesviral core NEC proteins are functionally conserved regarding complementarity of core NEC interactions, which were found either virus-specific or restricted within subfamilies.

ACS Style

Sigrun Häge; Eric Sonntag; Eva Maria Borst; Pierre Tannig; Lisa Seyler; Tobias Bäuerle; Susanne M. Bailer; Chung-Pei Lee; Regina Müller; Christina Wangen; Jens Milbradt; Manfred Marschall. Patterns of Autologous and Nonautologous Interactions between Core Nuclear Egress Complex (NEC) Proteins of α-, β- and γ-Herpesviruses. Viruses 2020, 12, 303 .

AMA Style

Sigrun Häge, Eric Sonntag, Eva Maria Borst, Pierre Tannig, Lisa Seyler, Tobias Bäuerle, Susanne M. Bailer, Chung-Pei Lee, Regina Müller, Christina Wangen, Jens Milbradt, Manfred Marschall. Patterns of Autologous and Nonautologous Interactions between Core Nuclear Egress Complex (NEC) Proteins of α-, β- and γ-Herpesviruses. Viruses. 2020; 12 (3):303.

Chicago/Turabian Style

Sigrun Häge; Eric Sonntag; Eva Maria Borst; Pierre Tannig; Lisa Seyler; Tobias Bäuerle; Susanne M. Bailer; Chung-Pei Lee; Regina Müller; Christina Wangen; Jens Milbradt; Manfred Marschall. 2020. "Patterns of Autologous and Nonautologous Interactions between Core Nuclear Egress Complex (NEC) Proteins of α-, β- and γ-Herpesviruses." Viruses 12, no. 3: 303.

Research
Published: 15 February 2018 in The FASEB Journal
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Although a vesicular nucleocytoplasmic transport system is believed to exist in eukaryotic cells, the features of this pathway are mostly unknown. Here, we report that the BFRF1 protein of the Epstein-Barr virus improves vesicular transport of nuclear envelope (NE) to facilitate the translocation and clearance of nuclear components. BFRF1 expression induces vesicles that selectively transport nuclear components to the cytoplasm. With the use of aggregation-prone proteins as tools, we found that aggregated nuclear proteins are dispersed when these BFRF1-induced vesicles are formed. BFRF1-containing vesicles engulf the NE-associated aggregates, exit through from the NE, and putatively fuse with autophagic vacuoles. Chemical treatment and genetic ablation of autophagy-related factors indicate that autophagosome formation and autophagy-linked FYVE protein-mediated autophagic proteolysis are involved in this selective clearance of nuclear proteins. Remarkably, vesicular transport, elicited by BFRF1, also attenuated nuclear aggregates accumulated in neuroblastoma cells. Accordingly, induction of NE-derived vesicles by BFRF1 facilitates nuclear protein translocation and clearance, suggesting that autophagy-coupled transport of nucleus-derived vesicles can be elicited for nuclear component catabolism in mammalian cells.—Liu, G.-T., Kung, H.-N., Chen, C.-K., Huang, C., Wang, Y.-L., Yu, C.-P., Lee, C.-P. Improving nuclear envelope dynamics by EBV BFRF1 facilitates intranuclear component clearance through autophagy. FASEB J. 32, 3968–3983 (2018). www.fasebj.org

ACS Style

Guan‐Ting Liu; Hsiu‐Ni Kung; Chung‐Kuan Chen; Cheng Huang; Yung‐Li Wang; Cheng‐Pu Yu; Chung‐Pei Lee. Improving nuclear envelope dynamics by EBV BFRF1 facilitates intranuclear component clearance through autophagy. The FASEB Journal 2018, 32, 3968 -3983.

AMA Style

Guan‐Ting Liu, Hsiu‐Ni Kung, Chung‐Kuan Chen, Cheng Huang, Yung‐Li Wang, Cheng‐Pu Yu, Chung‐Pei Lee. Improving nuclear envelope dynamics by EBV BFRF1 facilitates intranuclear component clearance through autophagy. The FASEB Journal. 2018; 32 (7):3968-3983.

Chicago/Turabian Style

Guan‐Ting Liu; Hsiu‐Ni Kung; Chung‐Kuan Chen; Cheng Huang; Yung‐Li Wang; Cheng‐Pu Yu; Chung‐Pei Lee. 2018. "Improving nuclear envelope dynamics by EBV BFRF1 facilitates intranuclear component clearance through autophagy." The FASEB Journal 32, no. 7: 3968-3983.

Journal article
Published: 01 February 2018 in Antiviral Research
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Hepatitis D virus (HDV) contains a single-stranded circular RNA genome that encodes two forms of hepatitis delta antigen (HDAg), the small delta antigen (HDAg-S) and the large delta antigen (HDAg-L). The two proteins have an identical amino acid sequence, except that HDAg-L has a 19-amino-acid extension at the C terminus. The domain spanning amino acid residues 198-210 of the HDAg-L (HDAg-L(198-210)) contains a nuclear export signal (NES), which is important for the nuclear export of HDV ribonucleoprotein to the cytoplasm. In this study, we established a cell permeable TAT-HA-HDAg-L(198-210) fusion protein using an E. coli protein expression system, to determine its function during HDV infection. The cytotoxicity of the TAT-HA-HDAg-L(198-210) fusion protein was investigated using an MTT assay, while a GST pull-down assay revealed that the TAT-HA-HDAg-L(198-210) fusion protein interfered with the interaction between HDAg-L and clathrin heavy chain (CHC). In addition, the cellular distribution of HDAg-L, in the presence of HBsAg, was observed by immunofluorescence staining and the TAT-HA-HDAg-L(198-210) fusion protein was found to impede the nuclear export of HDAg-L. Furthermore, assembly of HDV virus-like particles (VLPs) was decreased by the expression of the TAT-HDAg-L(198-210) fusion protein. The TAT-HA-HDAg-L(198-210) fusion protein also inhibited virus particle assembly and HDV secretion in a mouse model. These results suggest that the TAT-HA-HDAg-L(198-210) fusion protein inhibits the nuclear export of HDAg-L and competes with the C terminus of HDAg-L for interaction with CHC, and may have potential as a therapeutic agent for HDV infection.

ACS Style

Hsiu-Chen Huang; Hsu-Feng Lu; Yu-Heng Lai; Chung-Pei Lee; Hui-Kang Liu; Cheng Huang. Tat-enhanced delivery of the C terminus of HDAg-L inhibits assembly and secretion of hepatitis D virus. Antiviral Research 2018, 150, 69 -78.

AMA Style

Hsiu-Chen Huang, Hsu-Feng Lu, Yu-Heng Lai, Chung-Pei Lee, Hui-Kang Liu, Cheng Huang. Tat-enhanced delivery of the C terminus of HDAg-L inhibits assembly and secretion of hepatitis D virus. Antiviral Research. 2018; 150 ():69-78.

Chicago/Turabian Style

Hsiu-Chen Huang; Hsu-Feng Lu; Yu-Heng Lai; Chung-Pei Lee; Hui-Kang Liu; Cheng Huang. 2018. "Tat-enhanced delivery of the C terminus of HDAg-L inhibits assembly and secretion of hepatitis D virus." Antiviral Research 150, no. : 69-78.

Review
Published: 12 January 2010 in Reviews in Medical Virology
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The nuclear envelope of eukaryotic cells is composed of double lipid‐bilayer membranes, the membrane‐connected nuclear pore complexes and an underlying nuclear lamina network. The nuclear pore complexes serve as gates for regulating the transport of macromolecules between cytoplasm and nucleus. The nuclear lamina not only provides an intact meshwork for maintaining the nuclear stiffness but also presents a natural barrier against most DNA viruses. Herpesviruses are large DNA viruses associated with multiple human and animal diseases. The complex herpesviral virion contains more than 30 viral proteins. After viral DNA replication, the newly synthesised genome is packaged into the pre‐assembled intranuclear capsid. The nucleocapsid must then transverse through the nuclear envelope to the cytoplasm for the subsequent maturation process. Information regarding how nucleocapsid breaches the rigid nuclear lamina barrier and accesses the inner nuclear membrane for primary envelopment has emerged recently. From the point of view of both viral components and nuclear structure, this review summarises recent advances in the complicated protein–protein interactions and the phosphorylation regulations involved in the nuclear egress of herpesviral nucleocapsids. Copyright © 2010 John Wiley & Sons, Ltd.

ACS Style

Chung-Pei Lee; Mei-Ru Chen. Escape of herpesviruses from the nucleus. Reviews in Medical Virology 2010, 20, 214 -230.

AMA Style

Chung-Pei Lee, Mei-Ru Chen. Escape of herpesviruses from the nucleus. Reviews in Medical Virology. 2010; 20 (4):214-230.

Chicago/Turabian Style

Chung-Pei Lee; Mei-Ru Chen. 2010. "Escape of herpesviruses from the nucleus." Reviews in Medical Virology 20, no. 4: 214-230.