Research
Prions and Prion diseases
Prions are unconventional infectious pathogens that cause a variety of fatal neurodegenerative disorders in hosts. Prions are composed of protein termed PrPSc that is devoid of nucleic acids. This disease-associated PrPSc is a post-translationally misfolded isoform of PrPc encoded on PRNP gene locus and abundantly expressed in neurons. During prion pathogenesis, PrPSc (disease-asscociated rogue PrP) recruits and converts PrPC (cellular PrP with normal physiological function) to from nascent PrPSc. Conformational conversion of PrPC into the abnomally folded prion protein, PrPSc, is important for propagation of prions.
Prion diseases, also known as transmissible spongiform encephalopathies (TSE), include Cretzfelt-Jakob disease (CJD) in humans, bovine spongiform encephalopathy (BSE; mad cow disease) in cattle, scrapie in sheep and chronic wasting disease (CWD) in deer and elks. These diseases pose a potential risk for public health, but are incurable.
Research Topics
To develop therapy for prion diseases based on the understanding of mechanistic detail of prio propagation, the Laboratory preforms investigations on molecular aspects of prion and related disorders.
- Protein misfolding and neurodegenerative diseases
- Indentification of cellular factors that control prion propagation
- Molecular mechanism of prion replication
- Translational research form developing anti-prion therapy