Dr. Susanne Sievers

Senior Scientist, Group Leader

Department for Microbial Physiology and Molecular Biology

Felix-Hausdorff-Straße 8 - room-nr.: 1.49

17489 Greifswald

phone: +49 (0)3834 420 5900
fax:      +49 (0)3834 420 5909
email:   sieverss(at)uni-greifswald(dot)de

Curriculum Vitae
since 04/2021 Leader of the “Microbial Physiology & Molecular Biology” Group
02/2017 – 03/2021 group leader in the Institute of Microbiology, University Greifswald
02/2016 – 01/2017 maternity leave
04/2014 – 01/2016 post-doc with Katharina Riedel, University Greifswald
02/2013 – 03/2014 maternity leave
02/2011 – 01/2013 postdoctoral fellowship of the German research foundation with Birgitte Kallipolitis at the SDU, Odense, Denmark
02/2010 – 01/2011 maternity leave
07/2009 – 01/2010 postdoc in the group of Michael Hecker, University Greifswald
09/2005 – 07/2009 dissertation on the „Establishment and application of non-2-D gel-based techniques for identification and quantification of challenging protein classes in Gram-positive bacteria” with Michael Hecker, University of Greifswald
11/2003 – 03/2004 visiting researcher in the group of Ursula Jakob, University of Michigan, Ann Arbor, USA
10/2000 – 08/2005 study of Biochemistry, University of Greifswald
Research Interests
  • to investigate how the human pathogen Clostridium difficile responds to infection-relevant conditions and to compile proteomic  stress signatures in order to develop new weapons against this increasingly problematic pathogen

  • to elucidate the mechanistic details of C. difficile’s tolerance to oxygen and high concentrations of bile acids

  • to comprehensively describe alterations in thiol proteomes and identify specific cysteine modifications
Publications
  • Brauer M, Hotop SK, Wurster M, et al. Clostridioides difficile modifies its aromatic compound metabolism in response to amidochelocardin-induced membrane stress. mSphere. 2022 Sep-Oct; 7(5): e00302-22. PMID: 35993700
     
  • Metzendorf NG, Lange LM, Lainer N, et al. Destination and specific impact of different bile acids in the intestinal pathogen clostridioides difficile. Front Microbiol. 2022;13:814692. PMID: 35401433
     
  • Brauer M, Lassek C, Hinze C, et al. What’s a biofilm? -how the choice of the biofilm model impacts the protein inventory of clostridioides difficile. Front Microbiol. 2021;12:682111. PMID: 34177868
     
  • Troitzsch D, Zhang H, Dittmann S, et al. A point mutation in the transcriptional repressor perr results in a constitutive oxidative stress response in clostridioides difficile 630δerm. mSphere. 2021;6(2):e00091-21. PMID: 33658275
     
  • Karyolaimos A, Dolata KM, Antelo-varela M, et al. Escherichia coli Can Adapt Its Protein Translocation Machinery for Enhanced Periplasmic Recombinant Protein Production. Front Bioeng Biotechnol. 2019;7:465. PMID:32064253
     
  • Karyolaimos A, Ampah-korsah H, Hillenaar T, et al. Enhancing Recombinant Protein Yields in the Periplasm by Combining Signal Peptide and Production Rate Screening. Front Microbiol. 2019;10:1511. PMID:31396164
     
  • Sievers S, Metzendorf NG, Dittmann S, et al. Differential View on the Bile Acid Stress Response of . Front Microbiol. 2019;10:258.PMID:30833939
     
  • Guerrero montero I, Dolata KM, Schlüter R, et al. Comparative proteome analysis in an Escherichia coli CyDisCo strain identifies stress responses related to protein production, oxidative stress and accumulation of misfolded protein. Microb Cell Fact. 2019;18(1):19.PMID:30696436
     
  • Dolata KM, Montero IG, Miller W, et al. Far-reaching cellular consequences of tat deletion in Escherichia coli revealed by comprehensive proteome analyses. Microbiol Res. 2019;218:97-107.
     
  • Berges M, Michel AM, Lassek C, Nuss AM, Beckstette M, Dersch P, Riedel K, Sievers S, Becher D, Otto A, Maass S, Rohde M, Eckweiler D, Borrero-de Acuna JM, Jahn M, Neumann-Schaal M, Jahn D. Iron regulation in Clostridioides difficile. Front Microbiol. 2018. 9:3183. PMID:30619231
     
  • Sievers S. Membrane Proteomics in Gram-Positive Bacteria: Two Complementary Approaches to Target the Hydrophobic Species of Proteins. Methods Mol Biol. 2018;1841:21-33.PMID:30259477
     
  • Neumann-Schaal M, Metzendorf NG, Troitzsch D, Nuss AM, Hofmann JD, Beckstette M, Dersch P, Otto A, Sievers S. Tracking gene expression and oxidative damage of O-stressed Clostridioides difficile by a multi-omics approach. Anaerobe. 2018 May 31. pii: S1075-9964(18)30103-3 29859941.
     
  • Sievers S, Dittmann S, Jordt T, Otto A, Hochgräfe F, Riedel K. Comprehensive redox profiling of the thiol proteome of Clostridium difficile. Mol Cell Proteomics.2018 Mar 1. PMID: 29496906.
     
  • Otto A, Maaß S, Lassek C, Becher D, Hecker M, Riedel K, Sievers S. The protein inventory of Clostridium difficile grown in complex and minimal medium. Proteomics Clin Appl.2016 Oct;10(9-10):1068-1072. PMID: 27511832.
     
  • Sievers S, Lund A, Menendez-Gil P, Nielsen A, Storm Mollerup M, Lambert Nielsen S, Buch Larsson P, Borch-Jensen J, Johansson J, Kallipolitis BH. The multicopy sRNA LhrC controls expression of the oligopeptide-binding protein OppA in Listeria monocytogenes. RNA Biol.2015 Jul 15:0. PMID: 26176322.
  • Voigt B, Albrecht D, Sievers S, Becher D, Bongaerts J, Evers S, Schweder T, Maurer KH, Hecker M. High-resolution proteome maps of Bacillus licheniformis cells growing in minimal medium. Proteomics.2015 Apr 13. PMID: 25867794.
  • Sievers S, Sternkopf Lillebæk EM, Jacobsen K, Lund A, Mollerup MS, Nielsen PK, Kallipolitis BH. A multicopy sRNA of Listeria monocytogenes regulates expression of the virulence adhesin LapB. Nucleic Acids Res.2014 Aug;42(14):9383-98. PMID: 25034691.
     
  • Maass S, Sievers S, Zühlke D, Kuzinski J, Sappa PK, Muntel J, Hessling B, Bernhardt J, Sietmann R, Völker U, Hecker M, Becher D. Efficient, global-scale quantification of absolute protein amounts by integration of targeted mass spectrometry and two-dimensional gel-based proteomics. Anal Chem.2011 Apr 1;83(7):2677-84. PMID: 21395229.
     
  • Sievers S, Ernst CM, Geiger T, Hecker M, Wolz C, Becher D, Peschel A. Changing the phospholipid composition of Staphylococcus aureus causes distinct changes in membrane proteome and membrane-sensory regulators. Proteomics.2010 Apr;10(8):1685-93. PMID: 20162562.
     
  • Hempel K, Pané-Farré J, Otto A, Sievers S, Hecker M, Becher D. Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach. J Proteome Res.2010 Mar 5;9(3):1579-90. PMID: 20108986.
     
  • 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 JM, Hecker M. A proteomic view of an important human pathogen–towards the quantification of the entire Staphylococcus aureus proteome. PLoS One.2009 Dec 4;4(12):e8176. PMID: 19997597.
     
  • Hahne H, Wolff S, Hecker M, Becher D. From complementarity to comprehensiveness–targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics.2008 Oct;8(19):4123-36. PMID: 18763711.
     
  • Wolff S, Hahne H, Hecker M, Becher D. Complementary analysis of the vegetative membrane proteome of the human pathogen Staphylococcus aureus. Mol Cell Proteomics.2008 Aug;7(8):1460-8. PMID: 18460691.
     
  • Wolff S, Antelmann H, Albrecht D, Becher D, Bernhardt J, Bron S, Büttner K, van Dijl JM, Eymann C, Otto A, Tam le T, Hecker M. Towards the entire proteome of the model bacterium Bacillus subtilis by gel-based and gel-free approaches. J Chromatogr B Analyt Technol Biomed Life Sci.2007 Apr 15;849(1-2):129-40. PMID: 17055787.
     
  • Wolff S, Otto A, Albrecht D, Zeng JS, Büttner K, Glückmann M, Hecker M, Becher D. Gel-free and gel-based proteomics in Bacillus subtilis: a comparative study. Mol Cell Proteomics.2006 Jul;5(7):1183-92. PMID: 16552027.
     
  • Kohler C, Wolff S, Albrecht D, Fuchs S, Becher D, Büttner K, Engelmann S, Hecker M. Proteome analyses of Staphylococcus aureus in growing and non-growing cells: a physiological approach. Int J Med Microbiol.2005 Dec;295(8):547-65. PMID: 16325551.