Group Leader, Prion Cell Biology Research Lab
German Center for Neurodegenerative Diseases (DZNE)
D- 53127 Bonn
Phone +49 (0) 228 43302 6560
Curriculum vitae Prof. Dr. Ina Maja Vorberg
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. 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.
5 most important publications
1. Liu S, Hossinger A, Hofmann JP, Denner P, Vorberg IM. (2016) Horizontal transmission of cytosolic sup35 prions by extracellular vesicles. mBio, 7(4): e00915-16.
2. Hofmann JP, Denner P, Nussbaum-Krammer C, Kuhn P-H, Suhre MH, Scheibel T, Lichtenthaler SF, Schätzl HM, Bano D, Vorberg IM. (2013) Cell-to-cell propagation of infectious cytosolic protein aggregates. PNAS USA, 110: 5951-5956.
3. Krammer C, Kryndushkin D, Suhre MH, Kremmer E, Hofmann A, Pfeifer A, Scheibel T, Wickner RB, Schatzl HM, Vorberg I. (2009) The yeast Sup35NM domain propagates as a prion in mammalian cells. PNAS USA, 106: 462-467.
4. Vorberg I, Raines A, Story B, Priola SA. (2004) Susceptibility of common fibroblast cell lines to transmissible spongiform encephalopathy agents. J Infect Dis., 189: 431-439.
5. Vorberg I, Groschup MH, Pfaff E, Priola SA. (2003) Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. J Virol., 77: 2003-2009.