Institute of Novel and Emerging Infectious Diseases at the Friedrich Loeffler Institute

Greifswald, Germany

Institute of Novel and Emerging Infectious Diseases at the Friedrich Loeffler Institute

Greifswald, Germany
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Eiden M.,Institute of Novel and Emerging Infectious Diseases at the Friedrich Loeffler Institute | Vina-Rodriguez A.,Institute of Novel and Emerging Infectious Diseases at the Friedrich Loeffler Institute | Schlosser J.,Institute of Novel and Emerging Infectious Diseases at the Friedrich Loeffler Institute | Schirrmeier H.,Institute for Virus Diagnostic | Groschup M.H.,Institute of Novel and Emerging Infectious Diseases at the Friedrich Loeffler Institute
Food and Environmental Virology | Year: 2016

We detected Hepatitis E virus in serum samples of wild rabbits that were hunted in 1989 around the city of Greifswald, Germany. The recovery of one partial sequence and subsequent phylogenetic analysis indicates a close relationship to rabbit HEV sequences from France and suggests a long-established circulation of rabbit HEV in Europe. © 2015, Springer Science+Business Media New York.


PubMed | Institute of Novel and Emerging Infectious Diseases at the Friedrich Loeffler Institute and Institute for Virus Diagnostic
Type: Journal Article | Journal: Food and environmental virology | Year: 2016

We detected Hepatitis E virus in serum samples of wild rabbits that were hunted in 1989 around the city of Greifswald, Germany. The recovery of one partial sequence and subsequent phylogenetic analysis indicates a close relationship to rabbit HEV sequences from France and suggests a long-established circulation of rabbit HEV in Europe.


PubMed | Institute of Novel and Emerging Infectious Diseases at the Friedrich Loeffler Institute, Ludwig Maximilians University of Munich, University of Hamburg and University of Calgary
Type: Journal Article | Journal: Biochemical and biophysical research communications | Year: 2014

Prion diseases are fatal neurodegenerative disorders, which are not curable and no effective treatment exists so far. The major neuropathological change in diseased brains is the conversion of the normal cellular form of the prion protein PrPc(C) into a disease-associated isoform PrP(Sc). PrP(Sc) accumulates into multimeres and fibrillar aggregates, which leads to the formation of amyloid plaques. Increasing evidence indicates a fundamental role of PrP(Sc) species and its aggregation in the pathogenesis of prion diseases, which initiates the pathological cascade and leads to neurodegeneration accompanied by spongiform changes. In search of compounds that have the potential to interfere with PrP(Sc) formation and propagation, we used a cell based assay for the screening of potential aggregation inhibitors. The assay deals with a permanently prion infected cell line that was adapted for a high-throughput screening of a compound library composed of 10,000 compounds (DIVERset 2, ChemBridge). We could detect six different classes of highly potent inhibitors of PrP(Sc) propagation in vitro and identified piperazine derivatives as a new inhibitory lead structure, which increased incubation time of scrapie infected mice.

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