Prion Cell Biology
Prof. Dr. Ina Maja Vorberg
Group Leader
Venusberg-Campus 1, Gebäude 99
(ehemals Sigmund-Freud-Str. 27)
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

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
Krammer C, Kryndushkin D, Suhre MH, Kremmer E, Hofmann A, Pfeifer A, Scheibel T, Wickner RB, Schatzl HM, Vorberg I. The yeast Sup35NM domain propagates as a prion in mammalian cells. Proc Natl Acad Sci U S A. 2009 Jan 01; 106:462-7. doi: 10.1073/pnas.0811571106
Vorberg I, Raines A, Story B, Priola SA. Susceptibility of common fibroblast cell lines to transmissible spongiform encephalopathy agents. J Infect Dis. 2004 Jan 01; 189:431-9. doi: 10.1086/381166
Vorberg I, Groschup MH, Pfaff E, Priola SA. Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. J Virol. 2003 Jan 01; 77:2003-9.


Thursdays 1:30-4:30 pm

Patients +49 800-7799001

(free of charge)

Professionals +49 180-779900

(9 Cent/Min. German landline, mobile and out of Germany possibly more expensive)

Inform yourself on our website cookie-free. However, we would be pleased if you would allow us to use statistical cookies. Your browser settings regarding cookies are currently as follows:
More information can be found in our Privacy policy.