Research groupJunior group

Daniel Roderer

Structure and mechanism of microbiome-driven diseases

Portrait

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.


Profile

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. Meta-Omics 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. To close this major  gap of knowledge, we apply cryogenic electron microscopy (Cryo-EM) and single particle analysis to determine the structures of protein complexes that facilitate the host-microbiome interaction, a prerequisite for structure-based design of personalized anticancer compounds. To understand the context of how different adhesins act together in the cellular context, we apply cryo-ET to visualize molecular details of bacteria interacting with the host epithel and to integrate the in vitro structures into the in situ context.  

With numerous biological interactions involving membrane proteins and a general shortcoming of the underlying mechanistic details, the Roderer lab strives to decipher mechanistic details of action of membrane proteins and glycan-protein interactions. These include bacterial toxins that recognize human claudins at tight junctions, rhomboid proteases and their substrate recognition mechanism, and α5β1 integrin whose numerous glycosylation sites interact with and oligomerize galectin-3 in a conformational state-specific manner.  

Group Leader


The Roderer group

Alumni

Job Offers

If you are interested in a Master thesis position, please contact Daniel Roderer via email.

Plasmids deposited by the Roderer lab on Addgene

Publications via ORCID

Multi-state kinetics of the syringe-like injection mechanism of Tc toxins

  • Enrica Bordignon; Oleg Sitsel; Daniel Roderer; Daniel Prumbaum; Stefan Raunser; Min Dong; Claus Arthur Martin Seidel; Peter Njenga Ng'ang'a; Julian Folz; Svetlana Kucher; Ying Xu; Alexander Belyy; Ralf Kühnemuth; Tufa Enver Assafa

Science Advances 2025

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C. perfringens enterotoxin-claudin pore complex: Models for structure, mechanism of pore assembly and cation permeability

  • Santhosh Kumar Nagarajan; Joy Weber; Daniel Roderer; Jörg Piontek

Computational and Structural Biotechnology Journal 2025

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Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells

  • Felix Schöpf; Gian L. Marongiu; Klaudia Milaj; Thiemo Sprink; Judith Kikhney; Annette Moter; Daniel Roderer

Nature Communications 2025

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Nucleoside diphosphate kinase A (NME1) catalyses its own oligophosphorylation

  • Arif Celik; Felix Schöpf; Christian E. Stieger; Sarah Lampe; Björn Hanf; Jeremy A. M. Morgan; Max Ruwolt; Fan Liu; Christian P. R. Hackenberger; Daniel Roderer; Dorothea Fiedler

Nature Chemistry 2025

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Characterization of the direct and indirect inhibition of apoptosis by full-length recombinant Bcl-xL monomers

  • Christina Elsner; Ludovica M. Epasto; Adeline Cieren; Dominik Gendreizig; Svetlana Kucher; Daniel Roderer; Enrica Bordignon
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Structural basis for immune cell binding of Fusobacterium nucleatum via the trimeric autotransporter adhesin CbpF

  • Gian Luca Marongiu; Uwe Fink; Felix Schöpf; Andreas Oder; Jens Peter von Kries; Daniel Roderer

Proceedings of the National Academy of Sciences 2025

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Publications

  • M. Shafaq-Zadah*, E. Dransart, I. Hamitouche, 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. Nat Commun 16(1):9461; 2025. Doi: 10.1038/s41467-025-64523-7.
  • 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. Nat Commun 16(1):8104; 2025. Doi: 10.1038/s41467-025-63451-w.
  • G. L. Marongiu*, U. Fink*, F. Schöpf, A. Oder, J. P. von Kries and D. Roderer. Structural basis for immune cell binding of Fusobacterium nucleatum via the trimeric autotransporter adhesin CbpF. PNAS, 122(15), 2025. doi: 10.1073/pnas.2418155122.
  • 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. Multistate kinetics of the syringe-like injection mechanism of Tc toxins. Science Advances 11 (1), 2025. doi: 10.1126/sciadv.adr2019.
  • S.K. Nagarajan, J. Weber, D. Roderer and J. Piontek. C. perfringens enterotoxin-claudin pore complex: Models for structure, mechanism of pore assembly and cation permeability. Computational and Structural Biotechnology Journal 27 (287-306), 2025. doi: 10.1016/j.csbj.2024.11.048.
  • 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.
  • 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.
  • Y. Xu*, R. Viswanatha*, O. Sitsel, D. Roderer, H. Zhao, C. Ashwood, C. Voelcker, S. Tian, S. Raunser, N, Perrimon and M. Dong. CRISPR screens in Drosophila cells identify Vsg as a Tc toxin receptor. Nature 610 (349-355), 2022. doi: 10.1038/s41586-022-05250-7.
  • A. Belyy*, F. Lindemann*, D. Roderer, J. Funk, B. Bardiaux, J. Protze, P. Bieling, H. Oschkinat and S. Raunser. Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin. Nat Comm 13 (4202), 2022. doi: 10.1038/s41467-022-31836-w.
  • E. Mirgorodskaya, E. Dransart, M. Shafaq-Zadah, D. Roderer, C. Sihlbom, H. Leffler and L. Johannes. Site-specific N-glycan profiles of α5β1 integrin from rat liver. Biol. Cell 114 (6), 2022. doi: 10.1111/boc.202200017.
  • D. Roderer, F. Bröcker, O. Sitsel, P. Kaplonek, F. Leidreiter, P. H. Seeberger and S. Raunser. Glycan-dependent two-step cell adhesion mechanism of Tc toxins. Nat Comm 11 (2694), 2020. doi: 10.1038/s41467-020-16536-7.
  • D. Roderer, E. Schubert, O. Sitsel and S. Raunser. Towards the application of Tc toxins as a universal protein translocation system. Nat Comm 10, 5263 (2019). doi: 10.1038/s41467-019-13253-8.
  • D. Roderer, O. Hofnagel, R. Benz and S. Raunser. Structure of a Tc holotoxin pore provides insights into the translocation mechanism. PNAS 116 (45), 2019. doi: 10.1073/pnas.1909821116.
  • F. Leidreiter*, D. Roderer*, D. Meusch, C. Gatsogiannis and S. Raunser. Common architecture of Tc toxins from human and insect pathogenic bacteria. Science Advances 5 (10), 2019. doi: 10.1126/sciadv.aax6497.
  • D. Roderer and S. Raunser. Tc toxin complexes: Assembly, membrane permeation and protein translocation. Annual Review of Microbiology 73, 2019. doi: 10.1146/annurev-micro-102215-095531. Review.
  • T. Wagner, F. Merino, M. Stabrin, T. Moriya, C. Antoni, A. Apelbaum, P. Hagel, O. Sitsel, T. Raisch, D. Prumbaum, D. Quentin, D. Roderer, S. Tacke, B. Siebolds, E. Schubert, T.R. Shaikh, P. Lill, C. Gatsogiannis and S. Raunser. SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM. Communications Biology 2: 218, 2019. doi: 10.1038/s42003-019-0437-z.
  • C. Gatsogiannis*, F. Merino*, D. Roderer*, D. Balchin, E. Schubert, A. Kuhlee, M. Hayer-Hartl and S. Raunser. Tc toxin activation requires unfolding and refolding of a β-propeller. Nature 563 (209-213), 2018. doi: 10.1038/s41586-018-0556-6.
  • D. Roderer and R. Glockshuber. Assembly mechanism of the α-pore-forming toxin cytolysin A from Escherichia coli. Philos Trans R Soc Lond B Biol Sci. 5;372(1726), 2017. doi: 10.1098/rstb.2016.0211. Review.
  • C. Gatsogiannis, F. Merino, D. Prumbaum, D. Roderer, F. Leidreiter, D. Meusch and S. Raunser. Membrane insertion of a Tc toxin in near-atomic detail. Nat Struct Mol Biol 23 (10), 2016. doi: 10.1038/nsmb.3281.
  • D. Roderer, S. Benke, B. Schuler and R. Glockshuber. Soluble Oligomers of the Pore-forming Toxin Cytolysin A from Escherichia coli Are Off-pathway Products of Pore Assembly. J Biol Chem 291 (11), 2016. doi: 10.1074/jbc.M115.700757.
  • D. Roderer, R. Glockshuber and M. Rubini. Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline. ChemBioChem 16 (15), 2015. doi: 10.1002/cbic.201500342.
  • D. Roderer*, M Schärer*, M. Rubini and R. Glockshuber. Acceleration of protein folding by four orders of magnitude through a single amino acid substitution. SciRep 5 (11840), 2015. doi: 10.1038/srep11840.
  • S. Benke, D. Roderer, B. Wunderlich, D. Nettels, R. Glockshuber and B. Schuler. The assembly dynamics of the cytolytic pore toxin ClyA. Nat Comm 6 (6198), 2015. doi: 10.1038/ncomms7198.
  • D. Roderer, S. Benke, M. Müller, H. Fäh-Rechsteiner, N. Ban, B. Schuler and R. Glockshuber. Characterization of variants of the pore-forming toxin ClyA from Escherichia coli controlled by a redox switch. Biochemistry 53 (40), 2014. doi: 10.1021/bi5007578. 

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