Our research focuses on the molecular etiologies of human diseases caused by infection or genetic predisposition. Main projects at the moment focus on two areas of biology, namely the complement system alternative pathway (a part of the innate immune system) and a small oncogenic virus, Merkel cell polyomavirus.
We are structural biologists, with protein crystallography being the main technique in the lab. Most of the wet lab is concerned with the production and purification of difficult-to-produce (human and viral) proteins. Once pure protein is obtained we set up crystal trials and crystals are taken to the nearest synchrotron (the Swiss Light Source) for diffraction experiments. We employ NMR for the search of 'small molecule' ligands or, in the case of the virus work, inhibitors. Hits are again used for crystal soaking or co-crystallization and structural snapshots serve to design structure-informed mutations for functional studies.
We entertain a cryo electron microscopy collaboration but since the IFIB does not have a cryoEM students looking for in-depth EM training (or in-depth NMR training) are advised to ask for lab placements at the Tuebingen MPI campus.
The group is a member of the DFG research group ViroCarb.
Schmidt, C.Q.*, Ederveen, A.L.H., Harder, M.J., Wuhrer, M., Stehle, T., Blaum, B.S.* (2017). Biophysical analysis of sialic acid recognition by the complement regulator Factor H. Glycobiology doi: 10.1093/glycob/cwy061.
Blaum, B.S.* (2017). The lectin self of complement factor H. Curr Opin Struct Biol 44, 111-118.
Blaum, B.S.*, Frank, M., Walker, R.C., Neu, U., and Stehle, T. (2016). Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations. Glycobiology 26, 532-539.
Blaum, B.S.*, Hannan, J.P., Herbert, A.P., Kavanagh, D., Uhrin, D., and Stehle, T. (2015). Structural basis for sialic acid-mediated self-recognition by complement factor H. Nat Chem Biol 11, 77-82.
Neu, U., Allen, S.-A.A., Blaum, B.S., Liu, Y., Frank, M., Palma, A.S., Ströh, L.J., Feizi, T., Peters, T., Atwood, W.J., and Stehle, T. (2013). A structure-guided mutation in the major capsid protein retargets BK polyomavirus. PLoS Pathog 9, e1003688.
Neu, U., Hengel, H., Blaum, B.S., Schowalter, R.M., Macejak, D., Gilbert, M., Wakarchuk, W.W., Imamura, A., Ando, H., Kiso, M., Arnberg, N., Garcea, R.L., Peters, T., Buck, C.B., Stehle T. (2012). Structures of Merkel cell polyomavirus VP1 complexes define a sialic acid binding site required for infection. PLoS Pathog. 2012;8(7):e1002738.