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We are interested in the molecular mechanism of host-microbiome interactions in the human intestinal system, which play important roles in onset and progression of diseases. We therefore apply Cryo-EM to solve the structures of protein complexes that facilitate epithelial adhesion of bacteria.
We thrive to understand the molecular mechanism underlying the interaction of the intestinal microbiome with the human host. We focus on bacteria that are overrepresented in the microbiome of colorectal cancer (CRC) patients and the interactions of bacterial adhesins with epithelial and immune cells of the intestinal system. Genomic sequencing, big data analysis, and substantial microbial studies in animal models identified important drivers of CRC on the microbial and cellular level, but the underlying mechanistic details are not known. Therefore, we structurally analyze complexes between commensal proteins and human receptors to understand the molecular background of their binding mechanisms.
We apply cryogenic electron microscopy (Cryo-EM) and single particle analysis to determine the structures of protein complexes that facilitate the host-microbiome interaction, which is a prerequisite for structure-based design of personalized anticancer compounds. In addition, we visualize molecular details of bacteria interacting with the host epithel via cryo-ET to understand their binding mechanisms in a cellular context. Finally, we attempt to identify yet undescribed bacterial adhesins that facilitate epithelial binding in a pathogenic context using genomic and biochemical screening systems.
People
current position: Postdoc at Institut Curie, Paris.
current position: Cellular Imaging facility, FMP Berlin
If you are interested in a Master thesis position, please contact Daniel Roderer via email.
A. Celik, F. Schöpf, C.E. Sieger, J.A.M. Morgan, S. Lampe, M. Ruwolt, F. Liu, C.P.R. Hackenberger, D. Roderer and D. Fiedler. Nucleoside diphosphate kinase A (NME1) catalyzes its own oligophosphorylation. Preprint at bioRxiv, 2024. doi: 10.1101/2024.07.29.605581.
F. Schöpf, G. L. Marongiu, K. Milaj, T. Sprink, J. Kikhney, A. Moter and D. Roderer. Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells. Preprint at bioRxiv, 2024. doi: 10.1101/2024.02.28.582045 .
P. N. Ng’ang’a*, J. Folz*, S. Kucher*, D. Roderer*, Y. Xu, O. Sitsel, A. Belyy, D. Prumbaum, R. Kühnemuth, T. E. Assafa, M. Dong, C. A. M. Seidel, E. Bordignon and S. Raunser. Multi-state kinetics of the syringe-like injection mechanism of Tc toxins. Preprint at bioRxiv, 2024. doi: 10.1101/2024.01.16.575634
M. Shafaq-Zadah*, E. Dransart, C. Wunder, V. Chambon, C. A. Valades-Cruz, L. Leconte, N. Kumar Sarangi, J. Robinson, S. Bai, R. Regmi, A. Di Cicco, A. Hovasse, R. Bartels, U. Nilsson, S. Cianférani-Sanglier, H. Leffler, T. Keyes, D. Lévy, S. Raunser, D. Roderer*, L. Johannes*. Spatial N-glycan rearrangement on α5β1 integrin nucleates galectin-3 oligomers to determine endocytic fate. Preprint at bioRxiv, 2023. doi: 10.1101/2023.10.27.564026.
This text and the images are published under the Creative Commons licence "CC BY-NC-ND 4.0 EN - Attribution-Non-Commercial-No Derivative Works 4.0 Germany". Author: Daniel Roderer for leibniz-fmp.de
You may share the text by mentioning the licence CC BY-NC-ND 4.0 DE and the author(s). Copyright information on images/graphics/videos can be found directly with the images and additionally in the appendix.
The Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) is part of the Forschungsverbund Berlin e.V. (FVB), which legally represents seven non-university research institutes - members of the Leibniz Association - in Berlin.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10,
13125 Berlin, Germany
