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 EBV mutation literature information.


  Sequence variations of Epstein-Barr virus LMP1 gene in nasal NK/T-cell lymphoma.
 PMID: 16917737       2007       Virus genes
Abstract: In the epitopes ALLVLYSFA (codon 51-59), VLFIFGCLL (codon 110-118) and WLLLFLAIL (codon 173-181), several patients showed novel amino acid changes at codon 59 (Ala to Gly), 110 (Val to Leu) and 174 (Leu to Ile), respectively.
Abstract: In the major HLA-A2 restricted T-cell epitope sequence YLLEMLWRL (codon 125-133), all 7 patients showed amino acid changes at codon 126 (Leu to Phe) and 129 (Met to Ile).
Abstract: Within the NF-kB-activating domains, all 7 patients showed amino acid changes at codon 189 (Gln to Pro), 192 (Ser to Thr) and 212 (Gly to Ser) on either site of the PXQXT (codon 204-208) motif.


  Structural variability of the carboxy-terminus of Epstein-Barr virus encoded latent membrane protein 1 gene in Hodgkin's lymphomas.
 PMID: 17854036       2007       Journal of medical virology
Abstract: A distinct structural pattern was observed in del30 variants, characterized by a large number of 33 bp repeat units and the presence of a 15 bp insertion encoding the JAK3 Box-1a motif (3/15 wt vs. 16/20 del30; P = 0.001, chi(2) test).
Abstract: A higher frequency of del30 variant was observed in lymphomas (41/63) than in non-neoplastic controls (6/22) (OR 4.97, CI 95% 1.53-16.79; P = 0.005, chi(2) test). A large number (5-7) of 33 bp repeat units was characteristic of del30 LMP1 variants (P < 0.0001, Fisher's exact test).
Abstract: EBV association was characterized by EBER-ISH, LMP1 immunohistochemistry and PCR assays for EBNA2 and 3C (typing), LMP1 30 bp deletion (


  Phosphoacceptor site S173 in the regulatory domain of Epstein-Barr Virus ZEBRA protein is required for lytic DNA replication but not for activation of viral early genes.
 PMID: 17215287       2007       Journal of virology
Abstract: An independent assay based on ZEBRA solubility demonstrated a marked defect in DNA binding by the Z(S173A) mutant.
Abstract: The phenotype of a phosphomimetic mutant, the Z(S173D) mutant, was similar to that of wild-type ZEBRA.


  Multivalent sequence recognition by Epstein-Barr virus Zta requires cysteine 171 and an extension of the canonical B-ZIP domain.
 PMID: 16971443       2006       Journal of virology
Abstract: C171S disrupted Zta transcription activation function of several EBV lytic cycle promoters, including the BMRF1 gene (EA-D) and the other lytic activator, Rta.
Abstract: Overexpression of Rta could not rescue the C171S defect for transcription reactivation or viral DNA replication.
Abstract: Purified Zta C171S bound AP-1 sites similar to wild-type Zta, but it was incapable of binding several degenerate Zta sites, including a consensus C/EBP site.
Abstract: We found that serine substitution for cysteine 171 (


  Amino acids in the basic domain of Epstein-Barr virus ZEBRA protein play distinct roles in DNA binding, activation of early lytic gene expression, and promotion of viral DNA replication.
 PMID: 16940523       2006       Journal of virology
Abstract: Mutants competent to bind DNA could be separated into four functional groups: the wild-type group (eight mutants), a group defective at activating Rta (five mutants, all with mutations at the S186 site), a group defective at activating EA-D (three mutants with the R179A, S186T, and K192A mutations), and a group specifically defective at activating late gene expression (seven mutants).
Abstract: Three late mutants, with a Y180A, Y180E, or K188A mutation, were defective at stimulating EBV DNA replication.


  Regulation of the expression of the Epstein-Barr virus early gene BFRF1.
 PMID: 16406456       2006       Virology
Abstract: However, a co-operative effect between ZEBRA and RTA in the expression of BFRF1 is evident since the transfection of RTA can rescue the transactivating capacity of a mutant of the ZEBRA protein, known as Z(S186A), that has a substitution affecting the DNA binding region.


  Characterization of three essential residues in the conserved ATP-binding region of Epstein-Barr virus thymidine kinase.
 PMID: 15779905       2005       Biochemistry
Abstract: As the enzyme activity of G294A was reduced to 20% of that of wtTK, the K(m) for ATP binding of G294A was 48.7 microM as compared with 30.0 microM of EBV wtTK.
Abstract: EBV TK mutants K297E, K297Q, and K297R lost their ATP-binding ability and enzyme activity.
Abstract: However, K297R was shown to have a preference for usage of GTP (K(m): 43.0 microM) instead of ATP (K(m): 87.6 microM) as the phosphate donor.
Abstract: Interestingly, T298A retained its ATP-binding ability, suggesting a role of T298 in the catalytic process but not in the coordination of ATP.


  A redox-sensitive cysteine in Zta is required for Epstein-Barr virus lytic cycle DNA replication.
 PMID: 16227252       2005       Journal of virology
Abstract: C189S did provide some resistance to oxidation and nitrosylation, which potently inhibit Zta DNA binding activity in vitro.
Abstract: C189S was deficient for transcription activation of several viral late genes that depend on lytic replication and therefore was consistent with a primary defect of C189S in activating lytic replication.
Abstract: C189S was not defective in binding methylated DNA binding sites and was capable of activating Rta from endogenous latent viral genomes, in contrast to the previously characterized S186A mutation.
Abstract: C189S was slightly impaired for its ability to form a stable complex with Rta, although this did


  The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.
 PMID: 16160168       2005       Journal of virology
Abstract: Reduction in fusion activity was observed for mutants containing L65A and/or L69A mutations, while substitutions in L55 and L74 enhanced the fusion activity of the mutant gH/gL complexes with both cell types.


  BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186.
 PMID: 15919888       2005       Journal of virology
Abstract: A Z mutant containing an alanine residue at position 186 [Z(S186A)] was significantly defective in binding to methylated, as well as unmethylated, ZREs (Z-responsive elements) in Rp and was unable to activate lytic EBV gene transcription from the methylated or demethylated form of the viral genome.
Abstract: A Z mutant containing threonine at residue 186 [Z(S186T)] bound only to the methylated form of the ZRE-2 site in Rp and induced lytic EBV gene transcription from the methylated, but not demethylated, form of the viral genome.
Abstract: Finally, a Z mutant containing an aspartic acid at position 186 [Z(S186



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