Westfälische Wilhelms-University, University Hospital Münster
#50 - Institut für Hygiene
Contact
Team Leader: Dr. Thorsten Kuczius
Robert Koch Str. 41
Münster, 48149, Germany
Contact: Dr. Thorsten Kuczius
Tel: +49 2519802897
Fax: +49 2518355341
E-mail: tkuczius@uni-muenster.de
Institute website:
http://hygiene.klinikum.uni-muenster.de/
Main area of research
- Decontamination: Development of new and gentle inactivation techniques
- Prion characterization and differentiation: typing of prions isolated from different brain areas and various tissues and fluids; analyzing the influence on structural changes in regard to resistance to proteases by application of metal ions, detergents and by pH changes
- Analyses of prions in food
Research Team
- Researchers: 3
- Technicians: 2
- Postdocs: 0
- PHD/MD Students: 3
Facilities and Equipment
- Laboratories: BSL1, BSL2, BSL3
- General equipments: Photo-Imager
- Specific methods: High sensitive detection techniques of prion and brain marker proteins in biological samples, Precipitation techniques for prion enrichment
Main references
- Kuczius T, Koch R, Keyvani K, Karch H, Grassi J, Groschup MH. (2007). Regional and phenotype heterogeneity of cellular prion proteins in the human brain. Eur J Neurosci. 25:2649-2655.
- Kuczius T, Grassi J, Karch H, Groschup MH. (2007). Binding of N- and C-terminal anti-prion protein antibodies generates distinct phenotypes of cellular prion proteins (PrPC) obtained from human, sheep, cattle and mouse. FEBS J. 274:1492-1502.
- Kuczius T, Brinkmann B, Grassi J. (2007). Immunoreactivity enhancement with chelators for increasing the detection sensitivity of human PrPSc by Western blotting. Neurochem Int. 50:102-108.
- Kuczius T, Buschmann A, Zhang W, Karch H, Becker K, Peters G, Groschup MH. (2004). Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding.Biol Chem. 385:739-747.
- Kuczius T, Groschup MH. (1999). Differences in proteinase K resistance and neuronal deposition of abnormal prion proteins characterize bovine spongiform encephalopathy (BSE) and scrapie strains. Mol Med. 5:406-18.
- Kuczius T, Haist I, Groschup MH. (1998). Molecular analysis of bovine spongiform encephalopathy and scrapie strain variation. J Infect Dis. 178:693-9.
