Structural Biology of Cell Migration and Viral Infection

Everything in life is dynamic. Movement plays a fundamental role, from the level of whole organisms down to individual cells. Wound healing, embryonic development, fertilization and immune responses all rely on the cells' ability to move. Deregulation of these processes often leads to pathologies including tumor cell metastasis, developmental disorders and pathogen infection. The key player in the ability of cells to move is the so-called actin cytoskeleton. In the evolutionary arms race between host and pathogen, different bacteria and viruses have developed ways to hijack the cell’s own moving machinery to their own advantage, e.g. for infection, replication and spread.

The aim of our group is to obtain a detailed understanding of the structures in the dynamic environment of the actin cytoskeleton and its associated regulators in migrating cells, and in cases where pathogens (focusing on Vaccinia virus and Baculovirus) exploit actin-related host mechanisms. We are trying to understand how cells integrate external signals to form a complex network that allows them guided movement. This includes how both the cell and pathogens use important actin regulators such as the Arp2/3 complex and its upstream activators.

In order to structurally elucidate the molecular details underlying these processes we employ and will actively develop state-of-the-art correlative light and electron microscopy (CLEM), cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET) methods. These techniques allow us to visualize protein structures directly within their native environments (e.g. within melanoma cells), thus providing an understanding of the structure within its functional context. We additionally use novel images processing tools which have recently allowed us to obtain high-resolution structures from within pleomorphic virus particles and offer a unique potential towards cellular structural biology (see Schur FKM et al, 2016, Science, 353). We will continue these efforts to reveal the structure of other pleomorphic viruses at near-atomic detail, which will give important insights into the process of viral assembly.

The overarching goal of the group is to develop workflows that allow the structural characterization of transient membrane-proximal events, which so far have remained elusive due to lack of experimental tools, to study them in their native context. This includes how membrane complexes transduce signals from outside of the cell (e.g. chemokine gradients or other stimuli) onto intracellular networks, which is of critical importance for our understanding of cell biology.

Contact
Florian Schur
Institute of Science and Technology Austria (IST Austria)
Am Campus 1
A – 3400 Klosterneuburg
E-mail: florian.schur@remove-this.ist.ac.at

CV and Publication List

Florian Schur will join IST Austria in October 2017.

Assistant
Alexandra Mally

Phone: +43 (0)2243 9000-1105
E-mail: alexandra.mally@remove-this.ist.ac.at

Selected Publications

  • Schur FKM, Obr M, Hagen WJH, Wan W, Jakobi AJ, Kirkpatrick JM, Sachse C, Kräusslich H-G, Briggs JAG, (2016), An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation, Science, 353(6298):506-508
  • Mattei S*, Schur FKM*, Briggs JA, (2016). Retrovirus maturation - an extraordinary structural transformation. Current Opinion in Virology 18, 27-35.
  • Schur FKM, Hagen WJ, Rumlová M, Ruml T, Müller B, Kräusslich HG, Briggs JA. (2015). Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution. Nature 517:505-508.
  • Schur FKM*, Dick RA*, Hagen WJH, Vogt VM, Briggs JAG. (2015). The structure of the immature-like Rous sarcoma virus Gag particles reveals a structural role for the p10 domain in assembly. Journal of Virology. 89(20):10294-302.
  • Schur FKM, Hagen WJ, de Marco A, Briggs JA. (2013) Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging. Journal of Structural Biology. 184(3):394-400.
  • Koestler SA, Steffen A, Nemethova M, Winterhoff M, Luo N, Holleboom JM, Krupp J, Jacob, S, Vinzenz M, Schur F, Schlüter K, Gunning PW, Winkler C, Schmeiser C, Faix J, Stradal TEB, Small JV, Rottner K. (2013). Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin. Molecular Biology of the Cell. 24, 2861-2875.
  • Vinzenz M, Nemethova M, Schur F, Mueller J, Narita A, Urban E, Winkler C, Schmeiser C, Koestler SA, Rottner K, Resch GP, Maeda Y, Small JV. (2012). Actin branching in the initiation and maintenance of lamellipodia. Journal of Cell Science. 125, 2775-85

          *equal contribution

Career

Since 2017 Assistant Professor, IST Austria
2016-2017 Postdoc, European Molecular Biology Laboratory Heidelberg, Germany
2012-2016 PhD, European Molecular Biology Laboratory Heidelberg and University of Heidelberg, Germany
2010-2012 Diploma student/Research technician, Institute of Molecular Biology (IMBA), Vienna, Austria
2012 Magister “Molecular Biology”, Vienna University, Austria

Selected Distinctions

2016 Journal of Structural Biology, Paper of the year award 2016
2011 FEBS Youth Travel Fund award
2011 Poster prize, 26th Annual European Cytoskeleton Forum, "Actin-Based Motility: From Molecules to Model Organisms", Stresa/Italy

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