Christian Janzen
Christian Janzen
Christian Janzen is a molecular parasitologist whose main interest lies in chromatin-associated mechanisms during infection and development of protozoan parasites. He studied biology at the RWTH Aachen but moved to the University of Freiburg to receive his PhD in Virology. During his postdoctoral term at the Rockefeller University in New York he started to work on chromatin structure in African trypanosomes. In 2006, he became an independent group leader at the Ludwig-Maximilians-University (LMU) in Munich. Shortly after his habilitation in Genetics at the LMU in 2011, Christian Janzen was appointed Professor at the Department of Cell and Developmental Biology at the Julius-Maximilians-University in Wuerzburg.
since 2011 Professor for Developmental Biology, University of Würzburg
2011 Habilitation (Genetics), LMU Munich
2006-2011 Group Leader, LMU Munich
2001-2006 Postdoc, The Rockefeller University
2001 Dr. rer. nat (Biology), University Freiburg
1998 Diploma in Biology, RWTH Aachen
christian.janzen@uni-wuerzburg.de
Tel ++49 93131 86685
Students Tue, 4-6 p.m. Room C121
Research synopsis
Already as a student, Christian Janzen became fascinated by the sophisticated mechanisms that pathogens developed to invade the defence machinery of their hosts. After 3 months of field work in Uganda he decided to focus his future research on pathogens of tropical diseases. As a PhD student he tried to unravel how hemorrhagic RNA viruses turn off the interferon-induced host defence after infection. Christian Janzen continued to work on pathogen-host interactions when he started his post-doctoral studies. At the Rockefeller University, he established the foundations for current projects in his group with pioneer work on post-translational histone modifications and their influence on chromatin structure in African trypanosomes. Currently, Christian Janzen is using this parasite as a model organism to unravel how cells are able to adapt to extremely different environments when they shuttle between different host organisms. Trypanosomes have to adapt their morphology, metabolism and energy sources during a complex life cycle in different hosts and changes in chromatin structure and nuclear architecture have been observed during this process. Furthermore, he is interested in antigenic variation, a mechanism, which is essential for the parasite to evade the host’s immune response. Several nuclear proteins that are essential for these processes are in the focus of research in his laboratory. In a very fruitful collaboration with Dr. Falk Butter at the FLI in Greifswald, he employed high-throughput proteomic techniques to understand how changes in chromatin structure are regulated during developmental differentiation in T. brucei and why they are necessary for this process. The next challenge will be to transfer knowledge, techniques and expertise to answer similar questions in Leishmania parasites, which cause devastating diseases all over the world.
Selected Publications
A novel SNF2 ATPase complex in Trypanosoma brucei with a role in H2A.Z-mediated chromatin remodelling (2022) Vellmer T, Hartleb L, Fradera Sola A, Kramer S, Meyer-Natus E, Butter F, Janzen C PLoS Pathog. Jun 8;18(6):e1010514. doi: 10.1371/journal.ppat.1010514
A DOT1B/Ribonuclease H2 Protein Complex Is Involved in R-Loop Processing, Genomic Integrity, and Antigenic Variation in Trypanosoma brucei (2021) Eisenhuth N, Vellmer T, Rauh E, Butter F, Janzen C mBio Dec 21;12(6):e0135221. doi: 10.1128/mBio.01352-21
Cell-based and multi-omics profiling reveals dynamic metabolic repurposing of mitochondria to drive developmental progression of Trypanosoma brucei (2020) Doleželová E, Kunzová M, Dejung M, Levin M, Panicucci B, Regnault C, Janzen CJ, Barrett MP, Butter F, Zíková A.PLoS Biol. Jun 10;18(6):e3000741. doi: 10.1371/journal.pbio.3000741.
Genome maintenance functions of a putative Trypanosoma brucei translesion DNA polymerase include telomere association and a role in antigenic variation (2020) Leal AZ, Schwebs M, Briggs E, Weisert N, Reis H, Lemgruber L, Luko K, Wilkes J, Butter F, McCulloch R, Janzen C Nucleic Acids Res. Sep 25;48(17):9660-9680. doi: 10.1093/nar/gkaa686
Genome organization and DNA accessibility control antigenic variation in trypanosomes (2019) Müller L, Cosentino R, Förstner K, Guizetti J, Wedel C, Kaplan N, Janzen C, Arampatzi P, Vogel J, Steinbiss S, Otto D, Saliba A, Sebra R, Siegel N Nature Nov;563(7729):121-125.
TelAP1 links telomere complexes with developmental expression site silencing in African trypanosomes (2018) Reis H, Schwebs M, Dietz S, Janzen CJ, Butter F. Nucleic Acids Res. Jan 29. doi: 10.1093/nar/gky028
The nuclear proteome of Trypanosome brucei (2017) Goos C, Dejung M, Janzen CJ, Butter F, Kramer S. PLoS One. Jul 20;12(7):e0181884. doi: 10.1371/journal.pone.0181884.
Two flagellar BAR domain proteins in Trypanosoma brucei with stage-specific regulation (2016) Cicova Z, Dejung M, Skalicky T, Eisenhuth N, Hanselmann S, Morriswood B, Figueiredo LM, Butter F, Janzen CJ.
Sci Rep. Oct 25;6:35826. doi: 10.1038/srep35826.
Quantitative proteomics uncovers novel factors involved in developmental differentiation of Trypanosome brucei (2016)
Dejung M, Subota I, Bucerius F, Dindar G, Freiwald A, Engstler M, Boshart M, Butter F & Janzen CJ
PLoS Pathogen 12(2): doi:10.1371/journal.ppat.1005439
Structure-guided mutational analysis reveals the functional requirements for product specificity of DOT1 enzymes. (2014) Dindar G, Anger AM, Mehlhorn C, Hake SB, Janzen CJ.
Nat Commun. Nov 12;5:5313. doi: 10.1038/ncomms6313.
Comparative proteomics of two life cycle stages of stable isotope-labeled Trypanosoma brucei reveals novel components of the parasite's host adaptation machinery. (2013) Butter F, Bucerius F, Michel M, Cicova Z, Mann M, Janzen CJ.
Mol Cell Proteomics. Jan;12(1):172-9. doi: 10.1074/mcp.M112.019224.
DOT1A-dependent H3K76 methylation is required for replication regulation in Trypanosoma brucei (2012)
Gassen A, Brechtefeld D, Schandry N, Arteaga-Salas JM, Israel L, Imhof A, Janzen CJ.
Nucleic Acids Res. Nov 1;40(20):10302-11. doi: 10.1093/nar/gks801