Keynote Address III: Bettina Kempkes (13:00)

1:00 PM Keynote Address III Bettina Kempkes

Bettina Kempkes studied biology and graduated from the Albert-Ludwig
University Freiburg in 1986. She received her PhD at the Max-Planck
Institute of Immunobiology in Freiburg for her work on the T cell receptor
repertoire of hapten-specific T cells in 1989. Between 1989 and 1994 she
worked as a postdoctoral research fellow at the Helmholtz Center Munich.
From 1994 to 1996 she was a grantee of a fellowship for Research on
Infectious Diseases at the Cancer Center MGH Boston of Harvard Medical School. In 1996 she returned to the Helmholtz Center Munich and became a principal investigator and group leader of the team “Viral Latency”. 2002 she became an associate professor and 2006 an extra-ordinary professor for Molecular Tumor Biology at the Faculty of Biology at the Ludwigs-Maximilian University in Munich.

EBNA2 C-terminus new project
Harter …Song 2016 (PLoS Pathogens)  C-TAD EBNA2 in..

  • EBNA2 binds to the PLK1 serine/threonine kinase
  • PLK1: controls multiple processes in mitosis, also involved in check-point G2/S
  • PLK1 interacts with important regulator regions of EBNA2 (poster 174)
  • EBNA2 S460 and T468 are phosphorylation by PLK1 in Vito
  • S460A and T468V EBNA2 mutants show increased biological activity
  • Summary 2: PLK1is a target for cancer therapy thus could be a target for EBNA2 inactivation

Conclusion EBF1 anchors EBNA2 to chromatin…

Friberg A …. Kempkes B PLoS Pathogens 2015
  • The N-terminal dimerization domain of EBNA2 (END)
  • Hydrophobic interface of the dimer
  • Structural guided mutagenesis The EBNA2 interlace mutatnts L16D and I50D cannot form dimers
  • H15A and deflate alpha1 -helix form dimers but can not trans activation LMP1
  • Summary 2: The EBNA2 N terminal transactivation domain (END) folds into a dimeric structure required for
ER/EB2-5 system: EBNA2-estrogen receptor fusion protein needs estrogen to enter the nucleus and act (the EMBO paper)

EBNA2 target genes (RNA-seq on nuclear and cytoplasmic RNA fractions_ 6h post EBNA2 activation , in progress
  • Nucleus (5712) Cytoplasimc(4712?)
  • Cellular target genes of EBNA2 and EBNA3A nuclear fraction
  • 20% of EBNA2 cellular  targets are regulated by EBNA3A
  • TOP20 Ensemble gene Co-regulated by EBNA2 and 3A 
    • The MYC gene is flanked by genes of long non-coding RNAs that are c-regulated by EBNA2
EBNA2 regulates cellular gene expression in 
EBNA2 chromatin binding in CBF1 negative DG75
  • Normalized ChIP Data 
  • 82 TFs ENCODE 2012 GM12878, CBF1 Zhao et al 2011 EBNA2 Flag 
  • Signal intensities of EBNA2 correlate with CBF1 and EBF1 binding intensities
  • Early B cell factor
  • EBF family: EBF1, EBF2, EBF3, and 4
  • Within the hematopoietic system 
  • EBF1 independent EBNA2 chromatin binding sites: enriched for EBF1 motifs (DG75) and EEBF1 signals (GM12878)
  • CBF1 dep EBNA2 binding to chromatin is insensitive to EBF1 knock-down
  • EBF1 and EBNA2 physically interact in cellular protein complexes
    • (poster 167) the bindings require the protruding alpha-helix
EBNA3
  • The EBNA3 gene family members (3A, 3B, 3C) bind to B cell enhances and promoters and regulate transcription
  • Use cellular DNA anchors
    • Share a homologous domain that binds to CBF1 (RBPJ/CAL/SuH/Lag1)
    • Facilitate 
  • Delta EBNA3A initiate and maintain proliferation of primary human B cells (vs delta EBNA2 —> can’t proliferation)
  • EBNA3A positive and negative EBV infected B cells
    • CXCL10 is activated in 3A deletion (and 3C deletion, too)
  • CXCL10 and CXCL9 are repressed by 3A and 3C (both are located at Chromosome 4
  • PcG are located in the CXCL 9 and 10 loci (cool! 值得查一查)

Conditional EBNA-3A systems

  • PRTS1 -> Dox inducible 3A
  • Loss of Pol II/H3ac precedes the gain of repressive H3K27me3 marks and loss of activation marks H3K4me3 at the CXCL10 gene
    • Pol II, H3ac, H3K27me3, H3K4me3
    • 3A prevents binding of EBNA2 to enhancer regions
    • Repression of interferon induction of CXCL9 and CXCL10 by 3A is CBF1 dependent
    • CXCL10 and CXCL9 
    • Initiation of repression does not require CtBP
The model: It takes long time to relieve the PcG once 3A is removed

2.
Glaser LV, Rieger S, Thumann S, Beer S, Kuklik-Roos C, Martin DE, Maier KC, Harth-Hertle ML, Grüning B, Backofen R, Krebs S, Blum H, Zimmer R, Erhard F, Kempkes B.
PLoS Pathog. 2017 Oct 2;13(10):e1006664. doi: 10.1371/journal.ppat.1006664. eCollection 2017 Oct.
PMID:

 

28968461

 

Free PMC Article

3.
Daschkey S, Bienemann K, Schuster V, Kreth HW, Linka RM, Hönscheid A, Fritz G, Johannes C, Fleckenstein B, Kempkes B, Gombert M, Ginzel S, Borkhardt A.
J Clin Immunol. 2016 Oct;36(7):684-92. doi: 10.1007/s10875-016-0317-y. Epub 2016 Jul 29.
PMID:

 

27473539
4.
Gunnell A, Webb HM, Wood CD, McClellan MJ, Wichaidit B, Kempkes B, Jenner RG, Osborne C, Farrell PJ, West MJ.
Nucleic Acids Res. 2016 Jun 2;44(10):4636-50. doi: 10.1093/nar/gkw085. Epub 2016 Feb 15.
PMID:

 

26883634

 

Free PMC Article

5.
Kalchschmidt JS, Gillman AC, Paschos K, Bazot Q, Kempkes B, Allday MJ.
PLoS Pathog. 2016 Jan 11;12(1):e1005383. doi: 10.1371/journal.ppat.1005383. eCollection 2016 Jan.
PMID:

 

26751214

 

Free PMC Article

6.
Kempkes B, Robertson ES.
Curr Opin Virol. 2015 Oct;14:138-44. doi: 10.1016/j.coviro.2015.09.007. Review.
PMID:

 

26453799

 

Free PMC Article

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