Virusliterature

EBV mutation literature information.

Nasopharyngeal carcinoma risk prediction via salivary detection of host and Epstein-Barr virus genetic variants.

PMID: 29221111 2017 Oncotarget

Abstract: In this study, in southern China, where NPC is endemic, a single nucleotide polymorphism (SNP) in the EBV-encoded RPMS1 gene (locus 155391: G > A [G155391A]) and seven host SNPs (rs1412829, rs28421666, rs2860580, rs2894207, rs31489, rs6774494, and rs9510787) were confirmed to be significantly associated with NPC risk in 50 NPC cases versus 54 hospital-based controls with throat washing specimens and 1925 NPC cases versus 1947 hospital-based controls with buffy coat samples, respectively.

Method: The most striking finding was a significant association between a single nucleotide polymorphism (SNP) in the EBV-encoded RPMS1 gene (locus 155391: G

Epstein-Barr Virus Fusion with Epithelial Cells Triggered by gB Is Restricted by a gL Glycosylation Site.

PMID: 28956769 2017 Journal of virology

Abstract: Our previous study found that the gL glycosylation mutant N69L/S71V had an epithelial cell-specific hyperfusogenic phenotype.

Abstract: The gL_N69L/S71V mutant had a large increase in epithelial cell fusion activity of up to 300% greater than that of wild-type gL starting at early time points.

Clonal deleted latent membrane protein 1 variants of Epstein-Barr virus are predominant in European extranodal NK/T lymphomas and disappear during successful treatment.

PMID: 27061907 2016 International journal of cancer

Abstract: These results suggest that del30 may be associated with poor prognosis NK/TL and that strain evolution could be used as a potential marker to monitor treatment.

ERK2 phosphorylation of EBNA1 serine 383 residue is important for EBNA1-dependent transactivation.

PMID: 27009860 2016 Oncotarget

Abstract: In accordance, ERK2 was found to phosphorylate EBNA1 serine 383 in a reaction suppressed by H20 (a structural congener of the ERK inhibitor), U0126 (an inhibitor of MEK kinase), and mutations at substrate (S383A) or putative ERK docking sites.

Abstract: Wild-type (S383) and phosphomimetic (S383D) EBNA1 demonstrated comparable transactivation function, which was suppressed by H20 or U0126.

Method: Cytoplasmic and nuclear proteins from BJ-FE1 S383 WT, and S383A MT cells treated with DMSO and U0126 for 3 days were washed in 1 mL of ice cold PBS and then fractionated.

Method: Different EBNA1 constructs (387-641 WT, 379-~641 WT, or MTs of S383A, I528S,

A single nucleotide polymorphism in the Epstein-Barr virus genome is strongly associated with a high risk of nasopharyngeal carcinoma.

PMID: 26675171 2015 Chinese journal of cancer

Discussion: RPMS1 SNP G155391A was enriched in NPC patients but was not associated with other malignancies; these results support the hypothesis that there is a highly oncogenic EBV subtype specifically leading to NPC risk.

Discussion: In this multi-stage association study with a large sample size, we identified an EBV genomic sequence variation represented by RPMS1 SNP G155391A that was associated with a high risk of NPC.

Discussion: The frequency of RPMS1 SNP G155391A was significantly associated with the NPC incidence, and hig

Exosomal sorting of the viral oncoprotein LMP1 is restrained by TRAF2 association at signalling endosomes.

PMID: 25865256 2015 Journal of extracellular vesicles

Abstract: Notably, growth assays in soft agar revealed that oncogenic properties of the palmitoylation-deficient LMP1 mutant C78A were diminished compared to wild-type LMP1.

Method: HEK293 cells were transfected as described above with pGK2-LMP1wt or pGK2LMP1-C78A or pEGFP-N1.

Method: pGK2-LMP1-C78A was constructed by targeted mutagenesis of pGK2-LMP1wt, using the QuikChange Lightning Site-Directed Mutagenesis Kit protocol (Agilent, Santa Clara, CA, USA) and 5'-TTCAGAAGAGACCTTCTCGCTCCACTTGGAGCCCTTTG-3' as primer.

Discussion: One question remains: whether palmitoylation could actually promote LMP1 anchoring in late-endosomal membranes, as not all LMP1-C78A

RanBPM regulates Zta-mediated transcriptional activity in Epstein-Barr virus.

PMID: 25900136 2015 The Journal of general virology

Abstract: Interestingly, Z-K12R, a sumoylation-defective mutant of Zta, demonstrated transcriptional activation capabilities that were stronger than those of Zta and apparently unaffected by RanBPM modulation.

DNA Damage Signaling Is Induced in the Absence of Epstein-Barr Virus (EBV) Lytic DNA Replication and in Response to Expression of ZEBRA.

PMID: 25950714 2015 PloS one

Abstract: ZEBRA mutants deficient in DNA binding, Z(R183E) and Z(S186E), did not induce foci of pATM.

Method: After 8 h the transfection reagent was replaced with growth media and cells were incubated for another 24 hours.The lentivirus construct P3465V was kindly provided by Bill Sugden.

Method: PCR fragments were digested with BamH1 and EcoRI and ligated into the P3465V construct digested with BamH1 and EcoRI.

Method: The plasmids pHD1013/Z, pHD1013/Z(S186A), pHD1013/Z(S186E), pHD1013/Z(

Sequence analysis of Epstein-Barr virus (EBV) early genes BARF1 and BHRF1 in NK/T cell lymphoma from Northern China.

PMID: 26337172 2015 Virology journal

Result: At the transforming domain, only 1 more amino acid mutation was obtained in 1 isolate except for the V29A change.

Result: Considering the conservation of amino acid mutation and the mutual exclusion of mutations at the site of AA 79 and AA 88, the NK/T cell lymphoma cases were divided into 3 subtypes: 79V88V, 79L88L and 79V88L, the former two subtype carrying L88V, V79L mutations respectively, while the latter one without amino acid substitutions at these two residues.

Result: The

Result: The hottest V29A was detected at position 6 of epitope p23-31 or position 7 of p22-30 in 5 of 47 NK/T cell lymphoma isolates.

Nuclear translocation and regulation of intranuclear distribution of cytoplasmic poly(A)-binding protein are distinct processes mediated by two Epstein Barr virus proteins.

PMID: 24705134 2014 PloS one

Abstract: One ZEBRA mutant, Z(S186E), was deficient in translocation yet was capable of altering the intranuclear distribution of PABPC.

Result: 293 cells transfected with empty vector, or expression vectors for BGLF5, WT ZEBRA, Z(N182K), or Z(S186E) were analyzed for new protein synthesis.

Result: A ZEBRA mutant, Z(R183E), which induces nuclear aggregates and is concentrated in nuclear aggresomes, colocalized with PABPC within the nuclear aggregates and aggresomes when transfected in the absence of BGLF5

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