Contriving multiepitope subunit vaccine by exploiting structural and nonstructural viral proteins to prevent Epstein-Barr virus-associated malignancy

2018 ◽  
Vol 234 (5) ◽  
pp. 6437-6448 ◽  
Author(s):  
Rupal Ojha ◽  
Raj Nandani ◽  
Vijay Kumar Prajapati
Keyword(s):  
Subunit Vaccine ◽  
Epstein Barr Virus ◽  
Viral Proteins ◽  
Barr Virus ◽  
Associated Malignancy ◽  
Epstein Barr

scholarly journals Global Proteomic Changes Induced by the Epstein-Barr Virus Oncoproteins Latent Membrane Protein 1 and 2A

mBio ◽  
2018 ◽  
Vol 9 (3) ◽  
Author(s):  
Robert M. DeKroon ◽  
Harsha P. Gunawardena ◽  
Rachel Edwards ◽  
Nancy Raab-Traub
Keyword(s):  
Membrane Protein ◽  
Epstein Barr Virus ◽  
Viral Proteins ◽  
Latent Membrane Protein ◽  
Cellular Proteins ◽  
Latent Membrane Protein 1 ◽  
Barr Virus ◽  
Mediated Effects ◽  
Proteasome Subunits ◽  
Epstein Barr

ABSTRACTThe Epstein-Barr virus (EBV) oncoproteins latent membrane protein 1 (LMP1) and LMP2A constitutively activate multiple signaling pathways, and both have been shown to interact with cellular ubiquitin ligases and affect cellular ubiquitination. To detect the LMP1- and LMP2A-mediated effects on the global cellular proteome, epithelial cell lines expressing LMP1 or LMP2A were analyzed using label-free quantitative proteomics. To identify proteins whose ubiquitination is affected by the viral proteins, the cells were cultured in the presence and absence of deubiquitinase (DUB) and proteasome inhibitors. More than 7,700 proteins were identified with high confidence and considerably more proteins showed significant differences in expression in the presence of inhibitors. Few of the differentially expressed proteins with or without inhibitors were common between LMP1 and LMP2A, confirming that the viral proteins induce unique changes in cell expression and function. However, ingenuity pathway analysis (IPA) of the data indicated that LMP1 and LMP2A modulate many of the same cellular regulatory pathways, including cell death and survival, cell movement, and actin filament dynamics. In addition, various proteasome subunits, ubiquitin-specific peptidases and conjugating enzymes, vesicle trafficking proteins, and NF-κB and mitogen-activated protein kinase signaling proteins were affected by LMP1 or LMP2A. These findings suggest that LMP1 and LMP2A may commonly target critical cell pathways through effects on distinct genes, with many cellular proteins modified by ubiquitination and/or degradation.IMPORTANCEThe Epstein-Barr virus proteins latent membrane protein 1 and 2 have potent effects on cell growth and signaling. Both proteins bind to specific ubiquitin ligases and likely modulate the cellular proteome through ubiquitin-mediated effects on stability and intracellular location. In this study, a comprehensive proteomic analysis of the effects of LMP1 and LMP2A revealed that both proteins affected proteasome subunits, ubiquitin-specific conjugases and peptidases, and vesical trafficking proteins. The data suggest that the effects of these proteins on the abundance and ubiquitination of cellular proteins are in part responsible for their effects on cell growth regulation.

scholarly journals Epstein–Barr virus nuclear antigen 3A contains six nuclear-localization signals

2006 ◽  
Vol 87 (10) ◽  
pp. 2879-2884 ◽  
Author(s):  
Marion Buck ◽  
Anita Burgess ◽  
Roslynn Stirzaker ◽  
Kenia Krauer ◽  
Tom Sculley
Keyword(s):  
Nuclear Localization ◽  
Epstein Barr Virus ◽  
Fluorescent Protein ◽  
Viral Proteins ◽  
Site Directed Mutagenesis ◽  
Nuclear Antigen ◽  
Nuclear Localization Signals ◽  
Barr Virus ◽  
Epstein Barr

The Epstein–Barr nuclear antigen 3A (EBNA3A) is one of only six viral proteins essential for Epstein–Barr virus-induced transformation of primary human B cells in vitro. Viral proteins such as EBNA3A are able to interact with cellular proteins, manipulating various biochemical and signalling pathways to initiate and maintain the transformed state of infected cells. EBNA3A has been reported to have one nuclear-localization signal and is targeted to the nucleus during transformation, where it associates with components of the nuclear matrix. By using enhanced green fluorescent protein-tagged deletion mutants of EBNA3A in combination with site-directed mutagenesis, an additional five functional nuclear-localization signals have been identified in the EBNA3A protein. Two of these (aa 63–66 and 375–381) were computer-predicted, whilst the remaining three (aa 394–398, 573–578 and 598–603) were defined functionally in this study.

scholarly journals Early Detection of Nasopharyngeal Carcinoma

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Keiji Tabuchi ◽  
Masahiro Nakayama ◽  
Bungo Nishimura ◽  
Kentaro Hayashi ◽  
Akira Hara
Keyword(s):  
Nasopharyngeal Carcinoma ◽  
Early Detection ◽  
Epstein Barr Virus ◽  
Clinical Presentation ◽  
Southern China ◽  
Squamous Cell Carcinomas ◽  
Treatment Results ◽  
Barr Virus ◽  
Associated Malignancy ◽  
Epstein Barr

Nasopharyngeal carcinoma (NPC) is a unique disease with a clinical presentation, epidemiology, and histopathology differing from other squamous cell carcinomas of the head and neck. NPC is an Epstein-Barr virus-associated malignancy with a marked racial and geographic distribution. Specifically, it is highly prevalent in southern China, Southeast Asia, and the Middle East. To date, most NPC patients have been diagnosed in the advanced stage, but the treatment results for advanced NPC are not satisfactory. This paper provides a brief overview regarding NPC, with the focus on the early detection of initial and recurrent NPC lesions.

scholarly journals Viral proteins associated with the Epstein-Barr virus transactivator, ZEBRA.

1992 ◽  
Vol 89 (1) ◽  
pp. 378-382 ◽  
Author(s):  
D. A. Katz ◽  
R. P. Baumann ◽  
R. Sun ◽  
J. L. Kolman ◽  
N. Taylor ◽  
...  
Keyword(s):  
Epstein Barr Virus ◽  
Viral Proteins ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Epstein–Barr Virus BALF0 and BALF1 Modulate Autophagy

Viruses ◽  
2019 ◽  
Vol 11 (12) ◽  
pp. 1099
Author(s):  
Zhouwulin Shao ◽  
Chloé Borde ◽  
Frédérique Quignon ◽  
Alexandre Escargueil ◽  
Vincent Maréchal
Keyword(s):  
Cell Survival ◽  
Epstein Barr Virus ◽  
Viral Proteins ◽  
Open Reading Frame ◽  
Lytic Cycle ◽  
Reading Frame ◽  
Barr Virus ◽  
Viral Particles ◽  
Epstein Barr ◽  
Catabolic Process

Autophagy is an essential catabolic process that degrades cytoplasmic components within the lysosome, therefore ensuring cell survival and homeostasis. A growing number of viruses, including members of the Herpesviridae family, have been shown to manipulate autophagy to facilitate their persistence or optimize their replication. Previous works showed that the Epstein–Barr virus (EBV), a human transforming gammaherpesvirus, hijacked autophagy during the lytic phase of its cycle, possibly to favor the formation of viral particles. However, the viral proteins that are responsible for an EBV-mediated subversion of the autophagy pathways remain to be characterized. Here we provide the first evidence that the BALF0/1 open reading frame encodes for two conserved proteins of the Bcl-2 family, BALF0 and BALF1, that are expressed during the early phase of the lytic cycle and can modulate autophagy. A putative LC3-interacting region (LIR) has been identified that is required both for BALF1 colocalization with autophagosomes and for its ability to stimulate autophagy.

Mapping of B and T Cell Epitopes on the Epstein-Barr Virus Receptor Ligand Gp340: A Candidate Subunit Vaccine

1991 ◽  
pp. 207-211 ◽  
Author(s):  
Richard J. Pither ◽  
Chang X. Zhang ◽  
Lesley E. Wallace ◽  
Alan B. Rickinson ◽  
Andrew J. Morgan
Keyword(s):  
T Cell ◽  
Subunit Vaccine ◽  
Epstein Barr Virus ◽  
T Cell Epitopes ◽  
Receptor Ligand ◽  
Virus Receptor ◽  
Barr Virus ◽  
Epstein Barr
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