Miriam Kutsch, PhD
230 Jones Building
Durham, NC 27710
I studied Biochemistry at the Ruhr-University Bochum (RUB) in Germany. By joining the group of Christian Herrmann I had the opportunity to gain experience in purifying recombinant proteins and characterizing them with biochemical and biophysical techniques. In particular, I investigated members of the human guanylate-binding protein (hGBP) family which belong to the large GTPases. GBPs play important roles in the innate immune response against viral and bacterial pathogens. In order to move from investigating the molecular basis to investigate the biological functions of hGBPs I joined the group of Jörn Coers at Duke after earning my Doctor of Natural Sciences in Chemistry. My goal is to identify molecular mechanisms of antibacterial effects mediated by hGBPs using a combination of molecular biology, tissue culture and in vitro techniques.
I love to travel.
Kutsch M, Sistemich L, Lesser CF, Goldberg MB, Herrmann C & Coers J (2020) Direct binding of polymeric GBP1 to LPS disrupts bacterial cell envelope functions. EMBO J 39:e104926. doi: 10.15252/embj.2020104926
Kohler KM*, Kutsch M*, Piro AS*, Wallace GD, Coers J & Barber MF (2020) A Rapidly Evolving Polybasic Motif Modulates Bacterial Detection by Guanylate Binding Proteins. mBio 11:e00340-20. doi: 10.1128/mBio.00340-20 *shared first authorship
Ince S, Zhang P, Kutsch M, Krenczyk O, Shydlovskyi S & Herrmann C (2020) Catalytic Activity of Human Guanylate-Binding Protein 1 Coupled to the Release of Structural Restraints Imposed by the C-terminal Domain. FEBS J doi: 10.1111/febs.15348
Sistemich L, Kutsch M, Hämisch B, Zhang P, Shydlovskyi S, Britzen-Laurent N, Stürzl M, Huber K & Herrmann C (2020) The molecular mechanism of terminal triple-arginine motif of GBP1 inhibits actin-based motility. mBio polymer formation of farnesylated human guanylate-binding protein 1. J Mol Biol 432:2164-2185. doi: 10.1016/j.jmb.2020.02.009
Kutsch M, Ince S & Herrmann C (2018) Homo and hetero dimerisation of the human guanylate-binding proteins hGBP-1 and hGBP-5 characterised by affinities and kinetics. FEBS J 285:2019–2036. doi: 10.1111/febs.14459
Ince S*, Kutsch M*, Shydlovskyi S & Herrmann C (2017) The human guanylate-binding proteins hGBP-1 and hGBP-5 cycle between monomers and dimers only. FEBS J 284, 2284–2301. doi: 10.1111/febs.14126 *shared first authorship
Shydlovskyi S, Zienert AY, Ince S, Dovengerds C, Hohendahl A, Dargazanli JM, Blum A, Günther SD, Kladt N, Stürzl M, Schauss A, Kutsch M, Roux A, Praefcke GJK. & Herrmann C (2017) Nucleotide-dependent farnesyl switch orchestrates polymerization and membrane binding of human guanylate-binding protein 1. Proc Natl Acad Sci 114, E5559–E5568. doi: 10.1073/pnas.1620959114
Athanasopoulos PS, Jacob W, Neumann S, Kutsch M, Wolters D, Tan EK, Bichler Z, Herrmann C & Heumann R (2016) Identification of protein phosphatase 2A as an interacting protein of leucine-rich repeat kinase 2. Biological Chemistry 397, 6. doi: 10.1515/hsz-2015-0189
Kutsch M, Hortmann P, Herrmann C, Weibels S & Weingärtner H (2016) Dissecting ion-specific from electrostatic salt effects on amyloid fibrillation: A case study of insulin. Biointerphases 11, 019008. doi: 10.1116/1.4941008