EBV mutation literature information.


  BAMHI DNA fragment H-polymorphism of Epstein-Barr virus is associated with the mutations present in an 89 BP sequence localized in EBNA2 gene.
 PMID: 15215688       2004       Virus genes
Abstract: By nucleotide sequence analysis, we showed that there were two specific missense mutations in an 89 bp region of EBNA2 gene at position 49390-49479 of the EBV genome: a mutation at 49449 (C-->A) and another mutation at 49444 (T-->C), changing their amino acid sequence.


  Identification and characterization of the conserved nucleoside-binding sites in the Epstein-Barr virus thymidine kinase.
 PMID: 14705959       2004       The Biochemical journal
Abstract: For site 3, only mutants D392E (Asp392-->Glu) and R393H retain activity, indicating that a negative charge is important for Asp392 and a positive charge is required for Arg393.
Abstract: In site 4, the F402Y mutant retains full activity; however, F402S retains only 60% relative activity.
Abstract: Interestingly, the changed metal-ion usage pattern of D392E reveals that Asp392 plays multiple roles in this region.
Abstract: Strikingly, when Phe402 is substituted with serine residue, the original preferred pyrimidine substrates, such as 3'-azido-3'-deoxythymidine, iododeoxyuridine and beta-L-5-iododioxolane uracil (L-form substrate), have decreased competitiveness with thymidine, suggesting that Phe402 plays a crucial role


  Site-directed mutagenesis in a conserved motif of Epstein-Barr virus DNase that is homologous to the catalytic centre of type II restriction endonucleases.
 PMID: 12604820       2003       The Journal of general virology
Abstract: Biochemical analysis indicated that the preference for divalent cations was altered from Mg2+ to Mn2+ for mutant E225D.
Abstract: Five of these six variants retained nuclease activity and mutant D195N alone lost nuclease activity.
Abstract: However, K227 mutants were found to have variable DNA-binding abilities: K227G and K227N mutants retained, K227E and K227D had reduced and K227R lost DNA-binding ability.
Abstract: The DNA-binding abilities of D203E, E225D and E225Q were shown to be similar to that of wild-type.


  Disruption of Epstein-Barr virus latency in the absence of phosphorylation of ZEBRA by protein kinase C.
 PMID: 12388679       2002       Journal of virology
Abstract: Of greatest importance, in vivo labeling with [(32)P]orthophosphate showed that the tryptic phosphopeptide maps of wild-type ZEBRA, Z(S186A), and the double mutant Z(T159A/S186A) were identical.
Abstract: Studies in cell culture showed that phosphorylation of T159 was not required for disruption of latency in vivo, since the T159A mutant was fully functional.


  Epstein-Barr virus (EBV) subtype in EBV related oral squamous cell carcinoma in Okinawa, a subtropical island in southern Japan, compared with Kitakyushu and Kumamoto in mainland Japan.
 PMID: 12037022       2002       Journal of clinical pathology
Abstract: Sequence analysis of the type A virus EBNA2 gene revealed slight variations of the sequence (mutations)-(48991)G-->T and (48998)C-->A-in 18 of 33 cases compared with the B95-8 strain, and in 14 cases, in addition to these, a further mutation of (48917)T-->C was demonstrated; in the single remaining case, only one mutation at (49137)A-->G was detected.
Abstract: The (48991)G-->T and (48998)C-->A mutations of the EBNA2 region were demonstrated in type A virus, but the (48917)T-->C and (49137)A-->G mutations were not when compared with the B95-8 strain.
Abstract: The mutations at 48991 (G-->T), and 49137 (A-->G) are associated with amino acid changes Arg-->Met and Thr-->Ala, resp


  Differences in EBNA2 and LMP-1 carboxy terminal region sequences of Epstein-Barr virus type A between the tumors in a multiple cancer patient.
 PMID: 11432667       2001       Pathology, research and practice
Abstract: Although the squamous cell carcinoma of the tongue occurred after an interval of 18 years, the mutation site in the carcinomas was the same, 49137 (A-->G), as compared with B95-8 strain EBV EBNA2.
Abstract: The mutations at 48991 (G-->T) and 48998 (C-->A) were demonstrated in the lymphoma.


  [Increase of EGFR expression by Epstein-Barr virus LMP1 in nasopharyngeal carcinoma cells].
 PMID: 11783104       2001       Zhonghua zhong liu za zhi [Chinese journal of oncology]
Abstract: METHODS: Stable transfectant HNE2 cell line expressing LMP1 (HNE2-LMP1) or its mutants (HNE2 del 187-351, HNE2 1-231, HNE2 1-187) were used as cell models.


  Amino acid substitutions reveal distinct functions of serine 186 of the ZEBRA protein in activation of early lytic cycle genes and synergy with the Epstein-Barr virus R transactivator.
 PMID: 10233912       1999       Journal of virology
Abstract: A second class, represented by Z(S186C) and Z(S186G), was impaired in transcriptional activation, unable to activate early lytic cycle products from the latent virus, and not rescued by overexpression of Rta.
Abstract: A third class, Z(S186A), although unable by itself to activate BRLF1 or other lytic cycle genes, synergized with Rta.
Abstract: However, since Z(S186A) could synergize with Rta, synergy with Rta does not appear to be dependent on phosphorylation of S186.
Abstract: One


  Role of the epstein-barr virus RTA protein in activation of distinct classes of viral lytic cycle genes.
 PMID: 10559298       1999       Journal of virology
Abstract: The use of the Z(S186A) mutant form of ZEBRA, whose transactivation function is manifest only by coexpression of Rta, allows identification of a second class of lytic cycle genes, such as BMRF1 and BHRF1, that are activated in synergy by Rta and ZEBRA.


  EBNA-1 gene sequences in Brazilian and American patients with Hodgkin's disease.
 PMID: 10381519       1999       Blood
Abstract: Compared with the P-ala and P-thr cases, the V-leu cases were more likely to have the 30-bp latent membrane protein 1 (LMP1) gene deletion (P = 0.0075).
Abstract: In addition, cases of HD with the V-leu were statistically associated with a substitution of asparagine for glutamine at codon 322 of the C-terminal portion of the LMP1 gene.



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