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 EBV mutation literature information.


  Tetrameric ring formation of Epstein-Barr virus polymerase processivity factor is crucial for viral replication.
 PMID: 20926567       2010       Journal of virology
Abstract: Also, surprisingly, replication of the C206E virus, which is expected to have impairment of tail-to-tail contact, was severely restricted, although the mutant protein possesses the same in vitro biochemical activities as the wild type.
Abstract: The R256E virus, which has a severely impaired capacity for DNA binding and polymerase processivity, failed to form replication compartments, resulting in interference of viral replication, while the C95E mutation, which impairs head-to-head contact in vitro, unexpectedly hardly affected the viral replication.


  Conserved mutation of Epstein-Barr virus-encoded BamHI-A Rightward Frame-1 (BARF1) gene in Indonesian nasopharyngeal carcinoma.
 PMID: 20849661       2010       Infectious agents and cancer
Discussion: Another NPC tumor line derived from North-African origin, C15, even though demonstrating the V29A codon conversion, was also separated from most of the Indonesian NPC samples.
Discussion: Five mutations led to amino acid changes, mostly yielding conserved mutations of V29A (valine to alanine) and H130R (histidine to arginine).
Discussion: Furthermore, BARF1 variants with 2 amino acid changes (V29A and H130R) most commonly detected in EBV isolates from the NPC group which indicates this to be the dominant strain in Indonesian NPC.


  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.
Discussion: Z(S173A), also abolishes viral replication, while another substitution that maintains DNA binding.
Discussion: Z(S173D), h


  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.


  Comparative analysis of oncogenic properties and nuclear factor-kappaB activity of latent membrane protein 1 natural variants from Hodgkin's lymphoma's Reed-Sternberg cells and normal B-lymphocytes.
 PMID: 19211641       2009       Haematologica
Abstract: RESULTS: LMP1 variants of Reed-Sternberg cell origin were often associated with increased mutation rate and with recurrent genetic events, such as del15bp associated with S to N replacement at codon 309, and four substitutions I85L, F106Y, I122L, and M129I.


  Interaction of Epstein-Barr virus BZLF1 C-terminal tail structure and core zipper is required for DNA replication but not for promoter transactivation.
 PMID: 19144704       2009       Journal of virology
Abstract: The restoration of BZLF1 DNA replication activity by the complementation of two deleterious mutations (S208E and D236K) indicates that the interaction of the C-terminal tail and the core zipper is required for DNA replication, identifying a functional role for this structural feature unique to BZLF1.


  Two phenylalanines in the C-terminus of Epstein-Barr virus Rta protein reciprocally modulate its DNA binding and transactivation function.
 PMID: 19232420       2009       Virology
Abstract: Alanine substitution mutants, F600A/F605A, abolished activity of the DBIS.
Abstract: Alanine substitutions, F600A/F605A, decreased transcriptional activation by Rta protein, whereas aromatic substitutions, such as F600Y/F605Y or F600W/F605W, partially restored transcriptional activation.
Abstract: Full-length Rta protein with F600A/F605A mutations were enhanced in DNA binding compared to wild-type, whereas Rta proteins with F600Y/F605Y or


  The Epstein-Barr virus (EBV) deubiquitinating enzyme BPLF1 reduces EBV ribonucleotide reductase activity.
 PMID: 19244336       2009       Journal of virology
Abstract: Finally, expression of enzymatically active BPLF1 1-246 decreased RR activity, whereas a nonfunctional active-site mutant (BPLF1 C61S) had no effect.


  Epstein-Barr virus protein kinase BGLF4 interacts with viral transactivator BZLF1 and regulates its transactivation activity.
 PMID: 19321754       2009       The Journal of general virology
Abstract: In the present study, it was demonstrated that alanine substitution of the serine residue at position 209 (S209A) in BZLF1 eliminated phosphorylation of the protein by BGLF4 in vitro.
Abstract: The S209A mutation in BZLF1, as well as a K102I mutation in BGLF4, which inactivated catalytic activity of the viral kinase, also inhibited formation of a stable BGLF4-BZLF1 complex and downregulation of BZLF1 autotransactivation activity mediated by BGLF4.


  Methylation-dependent binding of the epstein-barr virus BZLF1 protein to viral promoters.
 PMID: 19325883       2009       PLoS pathogens
Abstract: The Z(S186A) mutant cannot activate methylated Nap in reporter gene assays and does not induce Na expression in cells with latent EBV infection.
Introduction: We also demonstrate that the CpG motifs in the Nap ZREs are usually methylated on the EBV genome during latent infection, and that a Z mutant, Z(S186A), which cannot bind to the methylated Nap ZREs in vitro is unable to activate Na expression in latently infected cells.
Method: Structures of Z bound to four different ZREs were modeled based on the crystal structure of Z (S186A, C189S) bound to the AP1 site (PDB code: 2c9l) using the Sybyl p



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