Protein-centric Discovery Tools

We develop chemical, biorthogonal, biochemical and proteomics strategies as ‘enabling discovery tools’ to gain novel insights into immune biology. We focus on approaches that capture molecular protein states that are not accessible with other omics technologies, such as interactions, sub-, and extracellular localizations and post-translational modifications.

• Our unbiased and sensitive secretomics method quantifies more than 50 cytokines and proteins with yet unknown extracellular functions released from rare primary cell populations. (Meissner et al 2013, Frauenstein et al 2018).
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• Our novel generation of MS cleavable isobaric mass (EASI) tags enables an unprecedentedly accurate quantification for virtually all proteomics applications on comparably cost-effective benchtop mass spectrometers (Virreira-Winter et al. 2018).
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• Our experimental and computational protein-centric framework establishes ‘social cellular communication networks’ based on ligand-receptor and receptor-receptor interactions an pinpoints intercellular signaling circuits altered in pathology (Rieckmann et al 2017).
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• Our combined genetic, pharmacological and biochemical secretomics approach dissects active secretory pathways, receptor shedding, extracellular vesicle, pore-formation, and membrane rupture-mediated protein release during programmed cell death (Tanzer et al 2020, Phulphagar et al 2021).
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• To define key proteins, their modifications, or physical and functional connections in immunological processes, we employ rigorous statistical methods and advanced computational approaches. Sharing of knowledge is an integral part of our research, and we conceive concepts to visualize high-dimensional data and make them publically available (see www.immprot.org).
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• Currently, we are expanding our intercellular signaling analyses to physiological systems in co-culture, organoids and in vivo, employing cell-type-specific labelling to define the cellular origin of proteins.
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• We are currently developing methods to identify receptors of previously unknown released proteins and post-translationally modified protein variants.