EBV mutation literature information.


  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.


  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: Rta rescued the capacity of Z(S186A) to activate the BMRF1 early lytic cycle gene from the latent virus.
Abstract: Z(S186A), a point mutant in ZEBRA
Abstract: A third class, Z(S186A), although unable by itself to activate BRLF1 or other lytic cycle genes, synergized with Rta.


  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.


  Rescue of the Epstein-Barr virus BZLF1 mutant, Z(S186A), early gene activation defect by the BRLF1 gene product.
 PMID: 9813214       1998       Virology
Abstract: Furthermore, we demonstrate that the ability of Z(S186A) to induce early BMRF1 and BHRF1 gene expression is rescued by cotransfection with a BRLF1 expression vector.
Abstract: However, the Z(S186A)/BRLF1 (R) combination cannot induce full lytic replication, suggesting that Z(S186A) may also be deficient in a replication-specific function.
Abstract: Recently, a serine-to-alanine mutation of Z residue 186 (within the basic DNA binding domain) was shown to inhibit the ability of Z to induce lytic infection in latently infected ce


  Alteration of a single serine in the basic domain of the Epstein-Barr virus ZEBRA protein separates its functions of transcriptional activation and disruption of latency.
 PMID: 9060666       1997       Journal of virology
Abstract: Therefore, initiation of the EBV lytic cycle by the ZEBRA protein requires a function in addition to transcriptional activation; a change of serine 186 to alanine in the DNA-binding domain of ZEBRA abolished this additional function and uncovered a new role for the ZEBRA protein in disruption of EBV latency.
Abstract: We generated a point mutant of ZEBRA, Z(S186A), that was not impaired in its ability to activate transcription; however, this mutation abolished its ability to initiate the viral lytic cascade.



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