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 EBV mutation literature information.


  Unique variations of Epstein-Barr virus-encoded BARF1 gene in nasopharyngeal carcinoma biopsies.
 PMID: 22406129       2012       Virus research
Abstract: V29A subtype, with one consistent amino acid change at residue 29 (V A) and several nucleotide changes, showed higher frequency in
Abstract: The relatively higher prevalence of type f/V29A/SPM strains in NPC may also suggest the association between these variations in multiple viral genes and NPC.
Abstract: Two major subtypes of BARF1 gene, designated as B95-8 and V29A, were identified.
Abstract: Type f isolates was specially correlated with the V29A/SPM genotype in NPC isolates and type f/V29A/SPM was preferentially found in NPC.


  Genomic sequencing and comparative analysis of Epstein-Barr virus genome isolated from primary nasopharyngeal carcinoma biopsy.
 PMID: 22590638       2012       PloS one
Abstract: Variations in LMP1 and EBNA3B epitopes and mutations in Cp (11404 C>T) and Qp (50134 G>C) found in GD1, GD2 and HKNPC1 could potentially affect CD8(+) T cell recognition and latent gene expression pattern in NPC, respectively.
Result: Although no mutations were identified in known and predicted TATA boxes, sequence changes of 11,324 G>T and 11,404 C>T in Cp, and 49,937 G>A and 50,134 G>C in Qp were observed.
Result: Based on strain-determining amino acids of EBNA1 (A487V, D499E and


  The Epstein-Barr virus-encoded BILF1 protein modulates immune recognition of endogenously processed antigen by targeting major histocompatibility complex class I molecules trafficking on both the exocytic and endocytic pathways.
 PMID: 21123379       2011       Journal of virology
Abstract: We now demonstrate that disruption of the EKT signaling motif of BILF1 by a K122A mutation impairs the ability of BILF1 to enhance endocytosis of surface MHC-I molecules, while subsequent lysosomal degradation was impaired by deletion of the 21-residue C-terminal tail of BILF1.


  Roscovitine inhibits EBNA1 serine 393 phosphorylation, nuclear localization, transcription, and episome maintenance.
 PMID: 21209116       2011       Journal of virology
Abstract: S393A mutant EBNA1 was deficient in supporting EBNA1- and oriP-dependent transcription and episome persistence, and roscovitine had little further effect on the diminished S393A mutant EBNA1-mediated transcription or episome persistence.
Abstract: Further, S393A mutation abrogated phosphorylation.
Abstract: Moreover, roscovitine decreased nuclear EBNA1 and often increased cytoplasmic EBNA1, whereas S393A mutant EBNA1 was localized equally in the nucleus and cytoplasm and was unaffected by roscovitine treatment.


  Efficient induction of nuclear aggresomes by specific single missense mutations in the DNA-binding domain of a viral AP-1 homolog.
 PMID: 21233201       2011       The Journal of biological chemistry
Abstract: Co-transfection of WT ZEBRA with aggresome-inducing mutants Z(R183E) and Z(R179E) inhibited late lytic viral protein expression and lytic viral DNA amplification.
Abstract: Four non-DNA-binding mutants, Z(R179E), Z(R183E), Z(R190E), and Z(K178D) localized to the periphery of large intranuclear spheres, to discrete nuclear aggregates, and to the cytoplasm.
Abstract: Other non-DNA-binding mutants, Z(N182K),


  Epstein-Barr virus nuclear protein 3C binds to the N-terminal (NTD) and beta trefoil domains (BTD) of RBP/CSL; only the NTD interaction is essential for lymphoblastoid cell growth.
 PMID: 21440926       2011       Virology
Abstract: Further, an EBNA3C WTP STP(W227S) mutation impaired BTD binding whereas EBNA3 homology domain mutations disrupted RBP/CSL N-terminal domain (NTD) binding.
Method: EBNA3C W227S was generated by Quickchange PCR (Stratagene, La Jolla, CA) and the mutated fragment cloned into the GST, pSG5-Flag and pCep EBNA3C wild-type plasmids to generate appropriate point mutants.
Method: Briefly, 7.5 x 106 EBNA3C-HT infected LCLs were transfected with 15 mug of oriP plasmid DNA expressing E3C, E3C W227S mutant, or control GFP oriP plasmid.
Result: EBNA3C binding to the beta trefoil domain containing constructs (B and B+C) was eliminated by


  Transmembrane peptides used to investigate the homo-oligomeric interface and binding hotspot of latent membrane protein 1.
 PMID: 21560118       2011       Biopolymers
Abstract: A full-length LMP-1 variant harboring the D150A substitution is deficient in NFkappaB activation, supporting the key role of the fifth transmembrane helix in constitutive activation of signaling by this oncoprotein.
Method: pRSV-LMP-1-D150A was generated using site-directed mutagenesis (Agilent Technologies 210519, CA, USA) to substitute D150 to alanine with the forward primer 5'-CCTAGCCTTCTTCCTAGCCCTCATCCTGCTC-3' and its reverse complement.
Method: pTox7 TM5 D150A was created using standard site directed mutagenesis with a commercially available Stratagene Quikchange II kit (Agilent, CA, USA).
Result: A population-based transcriptional reporter assay in HEp2 cells (Figure 6C) was used to determine if the D150A mutation attenuates


  Cellular transcription factor Oct-1 interacts with the Epstein-Barr virus BRLF1 protein to promote disruption of viral latency.
 PMID: 21697476       2011       Journal of virology
Abstract: In addition, we demonstrate that an Oct-1 mutant defective in DNA binding (the S335D mutant) still retains the ability to enhance BRLF1 transcriptional effects.
Abstract: We find that Oct-1 interacts directly with BRLF1 in vitro and that a mutant BRLF1 protein (the M140A mutant) attenuated for the ability to interact with Oct-1 in vitro is also resistant to Oct-1-mediated transcriptional enhancement in 293 BRLF1-stop cells.


  Transcriptional repression by sumoylation of Epstein-Barr virus BZLF1 protein correlates with association of histone deacetylase.
 PMID: 20516063       2010       The Journal of biological chemistry
Abstract: The K12R mutant of BZLF1, which no longer becomes sumoylated, exhibits stronger transactivation than the wild-type BZLF1 in a reporter assay system as well as in the context of virus genome with nucleosomal structures.


  A subset of replication proteins enhances origin recognition and lytic replication by the Epstein-Barr virus ZEBRA protein.
 PMID: 20808903       2010       PLoS pathogens
Abstract: A ZEBRA mutant, Z(S173A), at a phosphorylation site and three point mutants in the DNA recognition domain of ZEBRA, namely Z(Y180E), Z(R187K) and Z(K188A), were similarly deficient at activating lytic DNA replication and expression of late gene expression but were competent to activate transcription of viral early lytic genes.
Introduction: Additional proof for the role of phosphorylation of S173 in replication was attained when a phosphomimetic substitution mutant Z(S173D) activated both transcription and replication and was competent to bi



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