Prion Cell Biology
Prof. Dr. Ina Maja Vorberg
Group Leader
Venusberg-Campus 1/99
53127  Bonn
 +49 228 43302-560

Areas of investigation/research focus

Neurodegenerative diseases are associated with the aberrant folding of cellular proteins into highly ordered aggregates. Experimental evidence suggests that intercellularly transmitted protein aggregates can act as templates that induce the conformational transition of normally soluble protein into abnormally folded isoforms. This behavior is reminiscent of prions, infectious agents devoid of coding nucleic acid that cause transmissible spongiform encephalopathies in mammals. Our laboratory focuses on the molecular and cellular mechanisms involved in prion formation. We are particularly interested in cellular pathways involved in intercellular aggregate dissemination.

 more Infos

Conversion of normally soluble proteins into highly ordered aggregates is a hallmark of neurodegenerative diseases. Prion diseases or transmissible spongiform encephalopathies (TSE) are associated with misfolding of the cellular prion protein into infectious, self-templating entities. Prions replicate by converting monomeric prion protein into an infectious, aggregated isoform, capable of spreading within the affected host and between individuals.

Interestingly, aggregates with comparable propagation strategies have also been identified in lower eukaryotes where they induce heritable changes in progeny cells. Surprisingly, domains that compositionally resemble prototype yeast prion domains are abundant in the mammalian proteome. Aggregation of human proteins with so-called “prion-like domains” has been linked to several neurodegenerative diseases. If prion-like domains could confer true prion activities such as aggregate multiplication and spreading is so far unknown. Aim of our work is to understand general mechanisms of prion formation, clearance and intercellular dissemination. We employ high throughput cell-based assays, organotypic slice cultures and mouse models to characterize pathways involved in the replication of TSE agents and cytosolic proteins with prion-like domains.

Key Publications

Riemschoss K, Arndt V, Bolognesi B, von Eisenhart-Rothe P, Liu S, Buravlova O, Duernberger Y, Paulsen L, Hornberger A, Hossinger A, Lorenzo-Gotor N, Hogl S, Müller SA, Tartaglia G, Lichtenthaler SF, Vorberg IM. Fibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells. Life Sci Alliance. 2019 Jul 02; 2 doi: 10.26508/lsa.201800280
Duernberger Y, Liu S, Riemschoss K, Paulsen L, Bester R, Kuhn P-H, SchöllingM , Lichtenthaler S.F, Vorberg I. Prion Replication in the Mammalian Cytosol: Functional Regions within a Prion Domain Driving Induction, Propagation, and Inheritance. Mol Cell Biol. 2018 Jul 16; doi: 10.1128/MCB.00111-18
Rishibha Sachdev, Karin Kappes-Horn, Lydia Paulsen, Yvonne Duernberger, Catharina Pleschka, Philip Denner, Bishwajit Kundu, Jens Reimann, Ina Vorberg. Endoplasmic Reticulum Stress Induces Myostatin High Molecular Weight Aggregates and Impairs Mature Myostatin Secretion. Molecular Neurobiology. 2018 Oct 31; 55:8355-8373. doi: 10.1007/s12035-018-0997-9
Shu Liu, André Hossinger, Julia P. Hofmann, Philip Denner, Ina M. Vorberg. Horizontal transmission of cytosolic sup35 prions by extracellular vesicles. mBio. 2016 Jun 30; 7 doi: 10.1128/mBio.00915-16
Julia P. Hofmann, Philip Denner, Carmen Nussbaum-Krammer, Peer-Hendrik Kuhn, Michael H. Suhre, Thomas Scheibel, Stefan F. Lichtenthaler, Hermann M. Schätzl, Daniele Bano, Ina M. Vorberg. Cell-to-cell propagation of infectious cytosolic protein aggregates. Proceedings of the National Academy of Sciences of the United States of America. 2013 Apr 08; 110:5951-5956. doi: 10.1073/pnas.1217321110


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