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Westfälische Wilhelms-University, University Hospital Münster

Westfälische Wilhelms-University, University Hospital Münster

#50 - Institut für Hygiene

Dr. Thorsten Kuczius


Team Leader: Dr. Thorsten Kuczius
Robert Koch Str. 41
Münster, 48149, Germany
Contact: Dr. Thorsten Kuczius
Tel: +49 2519802897
Fax: +49 2518355341
Institute website:

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.

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