We use global as well as gene specific approaches to investigate the physiology of Staphylococcus aureus. We are particularly interested in the global adaptation of S. aureus to different growth limiting stress and starvation conditions – such as oxygen or carbon starvation.  In addition, to providing a global and quantitative view of the S. aureus physiology, these studies always identify a large number of proteins of unknown function. Therefore, in addition to the bird´s eye view provided by proteomics, we are also interested in the characterization of these proteins to uncover their molecular function in stress adaptation. During the last years it became evident that localization matters even in the seemingly simple world of bacterial cells. Consequently, a focus is put on the analysis of the spatial distribution of these proteins and how localization relates to function.

Furthermore, we are also interested in the evolution and function of signaling pathways controlled by the stressosome, a large 1.8 MDa cytosolic protein complex that was first described in the soil bacterium Bacillus subtilis. Using proteomics and phenotypic assays we map the biological processes controlled by the stressosome in Gram-negative bacteria including animal and plant pathogens to unravel the functional and regulatory diversity of the stressosome pathway.

2017 - 2021: Marie Skłodowska-Curie Innovative Training Network PATHSENSE, Role: Principal investigator (PI) of project: “Structure and role of the Vibrio vulnificus stressosome” 

2014 - 2018: DFG-Graduiertenkolleg 1870, Role: PI of project B2 “Expression and function of lipoproteins in Staphylococcus aureus” 

2014 - 2018: DFG- Sonderforschungsbereich Transregio 34, Co-Principal Investigator im Teilprojekt A08 “A systems biology perspective of regulatory and metabolic adaptation of Staphylococcus aureus to infection-related conditions”

 

Phenn J, Pané-Farré J, Meukow N, Klein A, Troitzsch A, Tan P, Fuchs S, Wagner GE, Lichtenegger S, Steinmetz I, Kohler C. RegAB Homolog of

Burkholderia pseudomallei is the Master Regulator of Redox Control and involved in Virulence. PLoS Pathog. 2021 May 28;17(5):e1009604. doi:

10.1371/journal.ppat.1009604.

 

Troitzsch A, Loi VV, Methling K, Zühlke D, Lalk M, Riedel K, Bernhardt J, Elsayed EM, Bange G, Antelmann H, Pané-Farré J. Carbon Source

Dependent Reprogramming of Anaerobic Metabolism in Staphylococcus aureus. J Bacteriol. 2021 Mar 23;203(8):e00639-20. doi:

10.1128/JB.00639-20.

 

Hinzke, T., Kleiner, M., Meister, M., Schlüter, R., Hentschker, C., Pané-Farré, J., Hildebrandt, P., Felbeck, H., Sievert, S. M., Bonn, F., Völker, U.,

Becher, D., Schweder, T., & Markert, S. (2021). Bacterial symbiont subpopulations have different roles in a deep-sea symbiosis. ELife.

https://doi.org/10.7554/elife.58371

 

Schwefel, K., Spiegler, S., Kirchmaier, B. C., Dellweg, P. K. E., Much, C. D., Pané-Farré, J., Strom, T. M., Riedel, K., Felbor, U., & Rath, M. (2020).

Fibronectin rescues aberrant phenotype of endothelial cells lacking either CCM1, CCM2 or CCM3. FASEB Journal.

https://doi.org/10.1096/fj.201902888R

 

Hook, J. C., Blagotinsek, V., Pané-Farré, J., Mrusek, D., Altegoer, F., Dornes, A., Schwan, M., Schier, L., Thormann, K. M., & Bange, G. (2020). A

Proline-Rich Element in the Type III Secretion Protein FlhB Contributes to Flagellar Biogenesis in the Beta- and Gamma-Proteobacteria. Frontiers in

Microbiology. https://doi.org/10.3389/fmicb.2020.564161

 

Petersen, I., Schlüter, R., Hoff, K. J., Liebscher, V., Bange, G., Riedel, K., & Pané-Farré, J. (2020). Non-invasive and label-free 3D-visualization

shows in vivo oligomerization of the staphylococcal alkaline shock protein 23 (Asp23). Scientific Reports. https://doi.org/10.1038/s41598-019-56907

9

 

Cutugno, L., Cafferty, J. M., Pané-Farré, J., O’byrne, C., & Boyd, A. (2020). Rpob mutations conferring rifampicin-resistance affect growth, stress

response and motility in vibrio vulnificus. Microbiology (United Kingdom). https://doi.org/10.1099/mic.0.000991

 

Graf, A. C., Leonard, A., Schäuble, M., Rieckmann, L. M., Hoyer, J., Maass, S., Lalk, M., Becher, D., Pané-Farré, J., & Riedel, K. (2019). Virulence

factors produced by staphylococcus aureus biofilms have a moonlighting function contributing to biofilm integrity. Molecular and Cellular Proteomics.

https://doi.org/10.1074/mcp.RA118.001120

 

Surmann, K., Depke, M., Dhople, V. M., Pané-Farré, J., Hildebrandt, P., Gumz, J., Schaible, U. E., Völker, U., & Schmidt, F. (2018). Analysis of

Staphylococcus aureus proteins secreted inside infected human epithelial cells. International Journal of Medical Microbiology.

https://doi.org/10.1016/j.ijmm.2018.06.002

 

Graf, A., Lewis, R. J., Fuchs, S., Pagels, M., Engelmann, S., Riedel, K., & Pané-Farré, J. (2018). The hidden lipoproteome of Staphylococcus

aureus. International Journal of Medical Microbiology. https://doi.org/10.1016/j.ijmm.2018.01.008

 

Binsker, U., Palankar, R., Wesche, J., Kohler, T. P., Prucha, J., Burchhardt, G., Rohde, M., Schmidt, F., Bröker, B. M., Mamat, U., Pané-Farré, J.,

Graf, A., Ebner, P., Greinacher, A., & Hammerschmidt, S. (2018). Secreted Immunomodulatory Proteins of Staphylococcus aureus Activate Platelets

and Induce Platelet Aggregation. Thrombosis and Haemostasis. https://doi.org/10.1055/s-0038-1637735

 

Fuchs, S., Mehlan, H., Bernhardt, J., Hennig, A., Michalik, S., Surmann, K., Pané-Farré, J., Giese, A., Weiss, S., Backert, L., Herbig, A., Nieselt, K.,

Hecker, M., Völker, U., & Mäder, U. (2018). AureoWiki ̵ The repository of the Staphylococcus aureus research and annotation community.

International Journal of Medical Microbiology. https://doi.org/10.1016/j.ijmm.2017.11.011

 

Loi, V. Van, Harms, M., Müller, M., Huyen, N. T. T., Hamilton, C. J., Hochgräfe, F., Pané-Farré, J., & Antelmann, H. (2017). Real-Time Imaging of the

Bacillithiol Redox Potential in the Human Pathogen Staphylococcus aureus Using a Genetically Encoded Bacilliredoxin-Fused Redox Biosensor.

Antioxidants and Redox Signaling. https://doi.org/10.1089/ars.2016.6733

 

Harris, J. R., & Jan Pané-Farré, Maureen B. Quin, Richard J. Lewis, J. M.-W. (2017). Macromolecular Protein Complexes. In Sub-Cellular

Biochemistry.

 

Pané-Farré, J., Quin, M. B., Lewis, R. J., & Marles-Wright, J. (2017). Structure and function of the stressosome signalling Hub. Sub-Cellular

Biochemistry. https://doi.org/10.1007/978-3-319-46503-6_1

 

Mäder, U., Nicolas, P., Depke, M., Pané-Farré, J., Debarbouille, M., van der Kooi-Pol, M. M., Guérin, C., Dérozier, S., Hiron, A., Jarmer, H., Leduc,

A., Michalik, S., Reilman, E., Schaffer, M., Schmidt, F., Bessières, P., Noirot, P., Hecker, M., Msadek, T., … van Dijl, J. M. (2016). Staphylococcus

aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions. PLoS Genetics.

https://doi.org/10.1371/journal.pgen.1005962

 

Bonn, F., Pané-Farré, J., Schlüter, R., Schaffer, M., Fuchs, S., Bernhardt, J., Riedel, K., Otto, A., Völker, U., van Dijl, J. M., Hecker, M., Mäder, U., &

Becher, D. (2016). Global analysis of the impact of linezolid onto virulence factor production in S. aureus USA300. International Journal of Medical

Microbiology. https://doi.org/10.1016/j.ijmm.2016.02.004

 

Vu, C. H., Kolata, J., Stentzel, S., Beyer, A., Gesell Salazar, M., Steil, L., Pané-Farré, J., Rühmling, V., Engelmann, S., Götz, F., van Dijl, J. M.,

Hecker, M., Mäder, U., Schmidt, F., Völker, U., & Bröker, B. M. (2016). Adaptive immune response to lipoproteins of Staphylococcus aureus in

healthy subjects. Proteomics. https://doi.org/10.1002/pmic.201600151

 

Liang, C., Schaack, D., Srivastava, M., Gupta, S. K., Sarukhanyan, E., Giese, A., Pagels, M., Romanov, N., Pané-Farré, J., Fuchs, S., & Dandekar,

T. (2016). A Staphylococcus aureus proteome overview: Shared and specific proteins and protein complexes from representative strains of all three

clades. Proteomes. https://doi.org/10.3390/proteomes4010008

 

Zühlke, D., Dörries, K., Bernhardt, J., Maaß, S., Muntel, J., Liebscher, V., Pané-Farré, J., Riedel, K., Lalk, M., Völker, U., Engelmann, S., Becher, D.,

Fuchs, S., & Hecker, M. (2016). Costs of life-Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis. Scientific Reports.

https://doi.org/10.1038/srep28172

 

Pförtner, H., Burian, M. S., Michalik, S., Depke, M., Hildebrandt, P., Dhople, V. M., Pané-Farré, J., Hecker, M., Schmidt, F., & Völker, U. (2014).

Activation of the alternative sigma factor SigB of Staphylococcus aureus following internalization by epithelial cells - An in vivo proteomics

perspective. International Journal of Medical Microbiology. https://doi.org/10.1016/j.ijmm.2013.11.014

 

Müller, M., Reiß, S., Schlüter, R., Mäder, U., Beyer, A., Reiß, W., Marles-Wright, J., Lewis, R. J., Pförtner, H., Völker, U., Riedel, K., Hecker, M.,

Engelmann, S., & Pané-Farré, J. (2014). Deletion of membrane-associated Asp23 leads to upregulation of cell wall stress genes in Staphylococcus

aureus. Molecular Microbiology. https://doi.org/10.1111/mmi.12733

 

Fuchs, S., Zühlke, D., Pané-Farré, J., Kusch, H., Wolf, C., Reiß, S., Binh, L. T. N., Albrecht, D., Riedel, K., Hecker, M., & Engelmann, S. (2013).

Aureolib - A Proteome Signature Library: Towards an Understanding of Staphylococcus aureus Pathophysiology. PLoS ONE.

https://doi.org/10.1371/journal.pone.0070669

 

Dangel, A., Ackermann, N., Abdel-Hadi, O., Maier, R., Önder, K., Francois, P., Müller, C. W., Pané-Farré, J., Engelmann, S., Schrenzel, J.,

Heesemann, J., & Lindermayr, C. (2013). A de novo-designed antimicrobial peptide with activity against multiresistant Staphylococcus aureus acting

on RsbW kinase. FASEB Journal. https://doi.org/10.1096/fj.13-234575

 

Lama, A., Pané-Farré, J., Chon, T., Wiersma, A. M., Sit, C. S., Vederas, J. C., Hecker, M., & Nakano, M. M. (2012). Response of methicillin-resistant

Staphylococcus aureus to amicoumacin a. PLoS ONE. https://doi.org/10.1371/journal.pone.0034037

 

Reiß, S., Pané-Farré, J., Fuchs, S., François, P., Liebeke, M., Schrenzel, J., Lindequist, U., Lalk, M., Wolz, C., Hecker, M., & Engelmann, S. (2012).

Global analysis of the Staphylococcus aureus response to mupirocin. Antimicrobial Agents and Chemotherapy. https://doi.org/10.1128/AAC.05363

11

 

Liebeke, M., Dörries, K., Zühlke, D., Bernhardt, J., Fuchs, S., Pané-Farré, J., Engelmann, S., Völker, U., Bode, R., Dandekar, T., Lindequist, U.,

Hecker, M., & Lalk, M. (2011). A metabolomics and proteomics study of the adaptation of Staphylococcus aureus to glucose starvation. Molecular

BioSystems. https://doi.org/10.1039/c0mb00315h

 

Lâm, T. T., Giese, B., Chikkaballi, D., Kühn, A., Wolber, W., Pané-Farré, J., Schäfer, D., Engelmann, S., Fraunholz, M., & Sinha, B. (2010).

Phagolysosomal integrity is generally maintained after Staphylococcus aureus invasion of nonprofessional phagocytes but is modulated by strain

6850. Infection and Immunity. https://doi.org/10.1128/IAI.00012-10

 

Hempel, K., Pané-Farré, J., Otto, A., Sievers, S., Hecker, M., & Becher, D. (2010). Quantitative cell surface proteome profiling for SigB-dependent

protein expression in the human pathogen Staphylococcus aureus via biotinylation approach. Journal of Proteome Research.

https://doi.org/10.1021/pr901143a

 

Pagels, M., Fuchs, S., Pané-Farré, J., Kohler, C., Menschner, L., Hecker, M., McNamarra, P. J., Bauer, M. C., von Wachenfeldt, C., Liebeke, M.,

Lalk, M., Sander, G., von Eiff, C., Proctor, R. A., & Engelmann, S. (2010). Redox sensing by a Rex-family repressor is involved in the regulation of

anaerobic gene expression in Staphylococcus aureus. Molecular Microbiology, 76(5), 1142–1161. https://doi.org/10.1111/j.1365-2958.2010.07105.x

 

Becher, D., Hempel, K., Sievers, S., Zühlke, D., Pané-Farré, J., Otto, A., Fuchs, S., Albrecht, D., Bernhardt, J., Engelmann, S., Völker, U., van Dijl,

J. M., & Hecker, M. (2009). A proteomic view of an important human pathogen-Towards the quantification of the entire staphylococcus aureus

proteome. PLoS ONE. https://doi.org/10.1371/journal.pone.0008176

 

Hain, T., Hossain, H., Chatterjee, S. S., MacHata, S., Volk, U., Wagner, S., Brors, B., Haas, S., Kuenne, C. T., Billion, A., Otten, S., Pane-Farre, J.,

Engelmann, S., & Chakraborty, T. (2008). Temporal transcriptomic analysis of the Listeria monocytogenes EGD-e σb regulon. BMC Microbiology.

https://doi.org/10.1186/1471-2180-8-20

 

Pané-Farré, J., Jonas, B., Hardwick, S. W., Gronau, K., Lewis, R. J., Hecker, M., & Engelmann, S. (2009). Role of RsbU in controlling SigB activity

in staphylococcus aureus following alkaline stress. Journal of Bacteriology. https://doi.org/10.1128/JB.01514-08

 

Hardwick, S. W., Pané-Farré, J., Delumeau, O., Marles-Wright, J., Murray, J. W., Hecker, M., & Lewis, R. J. (2007). Structural and functional

characterization of partner switching regulating the environmental stress response in Bacillus subtilis. Journal of Biological Chemistry.

https://doi.org/10.1074/jbc.M609733200

 

Fuchs, S., Pané-Farré, J., Kohler, C., Hecker, M., & Engelmann, S. (2007). Anaerobic gene expression in Staphylococcus aureus. Journal of

Bacteriology. https://doi.org/10.1128/JB.00081-07

 

Hecker, M., Pané-Farré, J., & Völker, U. (2007). SigB-dependent general stress response in Bacillus subtilis and related gram-positive bacteria. In

Annual Review of Microbiology. https://doi.org/10.1146/annurev.micro.61.080706.093445

 

Rogasch, K., Rühmling, V., Pané-Farré, J., Höper, D., Weinberg, C., Fuchs, S., Schmudde, M., Bröker, B. M., Wolz, C., Hecker, M., & Engelmann,

S. (2006). Influence of the two-component system SaeRS on global gene expression in two different Staphylococcus aureus strains. Journal of

Bacteriology. https://doi.org/10.1128/JB.00555-06

 

Pané-Farré, J., Jonas, B., Förstner, K., Engelmann, S., & Hecker, M. (2006). The σB regulon in Staphylococcus aureus and its regulation.

International Journal of Medical Microbiology. https://doi.org/10.1016/j.ijmm.2005.11.011

 

Pané-Farré, J., Lewis, R. J., & Stülke, J. (2005). The RsbRST stress module in bacteria: A signalling system that may interact with different output

modules. In Journal of Molecular Microbiology and Biotechnology. https://doi.org/10.1159/000088837