Epstein-Barr virus polymerase processivity factor enhances BALF2 promoter transcription as a coactivator for the BZLF1 immediate-early protein.
PMID: 19491105
2009
The Journal of biological chemistry
Abstract: A monomeric mutant, C95E, which is defective in homodimerization, could still interact and enhance BZLF1-mediated transactivation.
Crystal structure of epstein-barr virus DNA polymerase processivity factor BMRF1.
PMID: 19801550
2009
The Journal of biological chemistry
Abstract: Although the R87E and H141F mutants of BMRF1-DeltaC exhibited dramatically reduced polymerase processivity, they were still able to bind DNA and to dimerize.
Abstract: The C95E mutant, which disrupts dimer formation, lacked DNA binding activity, indicating that dimer formation is required for DNA binding.
Tumor-derived variants of Epstein-Barr virus latent membrane protein 1 induce sustained Erk activation and c-Fos.
PMID: 18986987
2008
The Journal of biological chemistry
Abstract: Point mutation of either amino acids 212 (glycine to serine) or 366 (serine to threonine) from the B95.8 isoform to the tumor variant version of LMP1 was sufficient for gain of function characterized by sustained activation of Erk and subsequent c-Fos induction and binding to the AP1 site.
Mutations of amino acids in the DNA-recognition domain of Epstein-Barr virus ZEBRA protein alter its sub-nuclear localization and affect formation of replication compartments.
Abstract: Co-expression of Rta with S186A mutant rescued diffuse EA-D but not globular replication compartments.
Abstract: The distribution of S186A mutant ZEBRA protein, defective for activation of Rta and EA-D, was identical to WT, except that the mutant ZEBRA was never found in globular compartments.
Abstract: The distribution of ZEBRA and EA-D proteins was identical to WT following transfection of K188R, a mutant with a conservative change.
Abstract: The most striking observation was that several mutant ZEBRA proteins defec
The reversal of epigenetic silencing of the EBV genome is regulated by viral bZIP protein.
PMID: 18631132
2008
Biochemical Society transactions
Abstract: ZtaC189S was not able to activate Rp in a B-cell line, demonstrating the relevance of the interaction with methylated ZREs.
Abstract: A single point mutant of Zta, C189S, is defective in binding to the methylated ZREs both in vitro and in vivo.
Methylated DNA recognition during the reversal of epigenetic silencing is regulated by cysteine and serine residues in the Epstein-Barr virus lytic switch protein.
Abstract: Zta's ability to trigger lytic cycle activation is severely compromised when a cysteine residue in its bZIP domain is mutated to serine (C189S), but the molecular basis for this effect is unknown.
Abstract: Here we show that the C189S mutant is defective for activating Rp in a Burkitt's lymphoma cell line.
Introduction: A previous study had shown that the point mutation S186A compromises Zta's ability to bind both the methylated and non-methylated forms of the ZREs within Rp.
Result: An independent mutation of C189 to alanine (ZtaC189A) also resulted in decreased binding to meZRE3, suggesting that the decreased binding of the C189S mutant was due to loss of the c
[Mutations of the Epstein-Barr virus LMP1 gene mutations in Russian patients with lymphoid pathology and healthy individuals].
Abstract: Among the point amino avid substitutions, the mutations S366T, F106Y, 185L, and E328Q associated with the enhanced transforming activity of a LMP1 molecule and its reduced cytotoxicity.
Epstein-Barr virus immediate-early protein Zta co-opts mitochondrial single-stranded DNA binding protein to promote viral and inhibit mitochondrial DNA replication.
Abstract: A point mutation in the Zta DNA binding domain (C189S), which is known to reduce lytic cycle replication, eliminated mtSSB association with Zta.
Genetic variations of EBV-LMP1 from nasopharyngeal carcinoma biopsies: potential loss of T cell epitopes.
PMID: 18297191
2008
Brazilian journal of medical and biological research
Abstract: Our study discovered that one of the 21 sequence variations harbored a new change at codon 131 (W-->C), and 5/21 specimens showed another novel change at codon 115 (G-->A) in the major epitope sequence of CD8+ T cells restricted by HLA-A2.
Abstract: Results showed that all 21 sequences displayed two amino acid changes most frequently in LMP1 of CD4+ T cell epitopes at codons 144 (F-->I, 21/21) and 212 (G-->S, 19/21) or (G-->N, 2/21).
Abstract: The other 3 sequences without this deletion all had a change at codon 344 (G-->D).
Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion.
Abstract: Substitution of alanine for glutamic acid at residue 595 reduces fusion with epithelial cells, greatly enhances fusion with B cells and allows low levels of B cell fusion even in the absence of gL.
Abstract: Substitution of alanine for glycine at residue 594 completely abrogates fusion with either B cells or epithelial cells.
EBV mutation literature information.
PMID: 
2009
The Journal of biological chemistry
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