scholarly journals A Major DNA Binding Protein Encoded by BALF2 Open Reading Frame of Epstein–Barr Virus (EBV) Forms a Complex with Other EBV DNA-Binding Proteins: DNAase, EA-D, and DNA Polymerase

Virology ◽  
1997 ◽  
Vol 239 (2) ◽  
pp. 285-295 ◽  
Author(s):  
Yué Zeng ◽  
Jaap Middeldorp ◽  
Jean-Jacques Madjar ◽  
Tadamasa Ooka
Keyword(s):  
Dna Binding ◽  
Dna Polymerase ◽  
Epstein Barr Virus ◽  
Dna Binding Protein ◽  
Dna Binding Proteins ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Barr Virus ◽  
Ebv Dna ◽  
Epstein Barr

scholarly journals Epstein–Barr Virus Single-Stranded DNA-Binding Protein: Purification, Characterization, and Action on DNA Synthesis by the Viral DNA Polymerase

Virology ◽  
1996 ◽  
Vol 222 (2) ◽  
pp. 352-364 ◽  
Author(s):  
Tatsuya Tsurumi ◽  
Akio Kobayashi ◽  
Katsuyuki Tamai ◽  
Hiroshi Yamada ◽  
Tohru Daikoku ◽  
...  
Keyword(s):  
Dna Binding ◽  
Dna Synthesis ◽  
Protein Purification ◽  
Dna Polymerase ◽  
Epstein Barr Virus ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Viral Dna ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Unexpected Absence of the Epstein-Barr Virus (EBV) lyLMP-1 Open Reading Frame in Tumor Virus Isolates: Lack of Correlation between Met129 Status and EBV Strain Identity

2003 ◽  
Vol 77 (7) ◽  
pp. 4415-4422 ◽  
Author(s):  
Kimberly D. Erickson ◽  
Christoph Berger ◽  
William F. Coffin ◽  
Edwin Schiff ◽  
Dennis M. Walling ◽  
...  
Keyword(s):  
Cell Lines ◽  
Epstein Barr Virus ◽  
Open Reading Frame ◽  
Lytic Cycle ◽  
Reading Frame ◽  
Barr Virus ◽  
Tumor Virus ◽  
Epstein Barr ◽  
Virus Isolates ◽  
Codon 129

ABSTRACT The lytic cycle-associated lytic latent membrane protein-1 (lyLMP-1) of Epstein-Barr virus (EBV) is an amino-terminally truncated form of the oncogenic LMP-1. Although lyLMP-1 shares none of LMP-1's transforming and signal transducing activities, we recently reported that lyLMP-1 can negatively regulate LMP-1-stimulated NF-κB activation. The lyLMP-1 protein encoded by the B95-8 strain of EBV initiates from methionine 129 (Met129) of the LMP-1 open reading frame (ORF). The recent report that Met129 in the B95-8 LMP-1 ORF is not conserved in the Akata strain of EBV prompted us to screen a panel of EBV-positive cell lines for conservation of Met129 and lyLMP-1 expression. We found that 15 out of 16 tumor-associated virus isolates sequenced encoded an ATT or ACC codon in place of ATG in the LMP-1 ORF at position 129, and tumor cell lines harboring isolates lacking an ATG at codon 129 did not express the lyLMP-1 protein. In contrast, we found that EBV DNA from 22 out of 37 healthy seropositive donors retained the Met129 codon. Finally, the lyLMP-1 initiator occurs variably within distinct EBV strains and its presence cannot be predicted by EBV strain identity. Thus, Met129 is not peculiar to the B95-8 strain of EBV, but rather can be found in the background of several evolutionarily distinct EBV strains. Its absence from EBV isolates from tumors raises the possibility of selective pressure on Met129 in EBV-dependent tumors.

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.

Establishment of a monkey kidney epithelial cell line with the BARF1 open reading frame from Epstein-Barr Virus

Oncogene ◽  
1997 ◽  
Vol 14 (25) ◽  
pp. 3073-3081 ◽  
Author(s):  
Ming Xin Wei ◽  
Mireille de Turenne-Tessier ◽  
Gisèle Decaussin ◽  
Gérard Benet ◽  
Tadamasa Ooka
Keyword(s):  
Epithelial Cell ◽  
Cell Line ◽  
Epstein Barr Virus ◽  
Open Reading Frame ◽  
Epithelial Cell Line ◽  
Reading Frame ◽  
Barr Virus ◽  
Kidney Epithelial Cell ◽  
Kidney Epithelial Cell Line ◽  
Epstein Barr

Structural features of the single-stranded DNA-binding protein of Epstein–Barr virus

2008 ◽  
Vol 161 (2) ◽  
pp. 172-187 ◽  
Author(s):  
E. Mumtsidu ◽  
A.M. Makhov ◽  
P.V. Konarev ◽  
D.I. Svergun ◽  
J.D. Griffith ◽  
...  
Keyword(s):  
Dna Binding ◽  
Epstein Barr Virus ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Structural Features ◽  
Single Stranded Dna ◽  
Barr Virus ◽  
Epstein Barr

Epstein-Barr virus-related DNA-binding proteins induced by n-butyrate in P3HR-1 cells

Virology ◽  
1982 ◽  
Vol 116 (1) ◽  
pp. 354-358 ◽  
Author(s):  
Kenji Sugawara ◽  
Michiko Kawanishi ◽  
Yohei Ito
Keyword(s):  
Dna Binding ◽  
Epstein Barr Virus ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Epstein–Barr virus nuclear antigen 1 is a DNA-binding protein with strong RNA-binding activity

2004 ◽  
Vol 85 (10) ◽  
pp. 2755-2765 ◽  
Author(s):  
Chih-Chung Lu ◽  
Chia-Wei Wu ◽  
Shin C. Chang ◽  
Tzu-Yi Chen ◽  
Chwan-Ren Hu ◽  
...  
Keyword(s):  
Dna Binding ◽  
Epstein Barr Virus ◽  
Rna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Binding Activity ◽  
Nuclear Antigen ◽  
Barr Virus ◽  
Infected Cells ◽  
Epstein Barr

Epstein–Barr virus (EBV) nuclear antigen 1 (EBNA-1) plays key roles in both the regulation of gene expression and the replication of the EBV genome in latently infected cells. To characterize the RNA-binding activity of EBNA-1, it was demonstrated that EBNA-1 binds efficiently to RNA homopolymers that are composed of poly(G) and weakly to those composed of poly(U). All three RGG boxes of EBNA-1 contributed additively to poly(G)-binding activity and could mediate RNA binding when attached to a heterologous protein in an RNA gel mobility-shift assay. In vitro-transcribed EBV and non-EBV RNA probes revealed that EBNA-1 bound to most RNAs examined and the affinity increased as the content of G and U increased, as demonstrated in competition assays. Among these probes, the 5′ non-coding region (NCR) (nt 131–278) of hepatitis C virus RNA appeared to be the strongest competitor for EBNA-1 binding to the EBV-encoded small nuclear RNA 1 (EBER1) probe, whereas a mutant 5′ NCR RNA with partially disrupted secondary structure was a weak competitor. Furthermore, the interaction of endogenous EBNA-1 and EBER1 in EBV-infected cells was demonstrated by a ribonucleoprotein immunoprecipitation assay. These results revealed that EBNA-1 is a DNA-binding protein with strong binding activity to a relatively broad spectrum of RNA and suggested an additional biological impact of EBNA-1 through its ability to bind to RNA.

scholarly journals Epstein-Barr Virus BamHI-A Rightward Transcript-Encoded RPMS Protein Interacts with the CBF1-Associated Corepressor CIR To Negatively Regulate the Activity of EBNA2 and NotchIC

2001 ◽  
Vol 75 (6) ◽  
pp. 2946-2956 ◽  
Author(s):  
Jinxia Zhang ◽  
Honglin Chen ◽  
Gerry Weinmaster ◽  
S. Diane Hayward
Keyword(s):  
Cell Lines ◽  
Epstein Barr Virus ◽  
Intracellular Localization ◽  
Open Reading Frame ◽  
Negative Regulator ◽  
Reading Frame ◽  
Barr Virus ◽  
Corepressor Complex ◽  
Epstein Barr ◽  
Two Hybrid

ABSTRACT The Epstein-Barr virus (EBV) BamHI-A rightward transcripts (BARTs) are expressed in all EBV-associated tumors as well as in latently infected B cells in vivo and cultured B-cell lines. One of the BART family transcripts contains an open reading frame, RPMS1, that encodes a nuclear protein termed RPMS. Reverse transcription-PCR analysis revealed that BART transcripts with the splicing pattern that generates the RPMS1 open reading frame are commonly expressed in EBV-positive lymphoblastoid cell lines and are also detected in Hodgkin's disease tissues. Experiments undertaken to determine the function of RPMS revealed that RPMS interacts with both CBF1 and components of the CBF1-associated corepressor complex. RPMS interaction with CBF1 was demonstrated in a glutathione S-transferase (GST) affinity assay and by the ability of RPMS to alter the intracellular localization of a mutant CBF1. A Gal4-RPMS fusion protein mediated transcriptional repression, suggesting an additional interaction between RPMS and corepressor proteins. GST affinity assays revealed interaction between RPMS and the corepressor Sin3A and CIR. The RPMS-CIR interaction was further substantiated in mammalian two-hybrid, coimmunoprecipitation, and colocalization experiments. RPMS has been shown to interfere with NotchIC and EBNA2 activation of CBF1-containing promoters in reporter assays. Consistent with this function, immunofluorescence assays performed on cotransfected cells showed that there was colocalization of RPMS with NotchIC and with EBNA2 in intranuclear punctate speckles. The effect of RPMS on NotchIC function was further examined in a muscle cell differentiation assay where RPMS was found to partially reverse NotchIC-mediated inhibition of differentiation. The mechanism of RPMS action was examined in cotransfection and mammalian two-hybrid assays. The results revealed that RPMS blocked relief of CBF1-mediated repression and interfered with SKIP-CIR interactions. We conclude that RPMS acts as a negative regulator of EBNA2 and Notch activity through its interactions with the CBF1-associated corepressor complex.

scholarly journals Characterization of Epstein-Barr Virus DNase and Its Interaction with the Major DNA Binding Protein

Virology ◽  
1995 ◽  
Vol 208 (2) ◽  
pp. 712-722 ◽  
Author(s):  
Su-Fang Lin ◽  
Tsuey-Ying Hsu ◽  
Mei-Ying Liu ◽  
Lung-Shen Lin ◽  
Huey-Lang Yang ◽  
...  
Keyword(s):  
Dna Binding ◽  
Epstein Barr Virus ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Barr Virus ◽  
Epstein Barr
Sign in / Sign up

Export Citation Format

Share Document