Speaker
Description
Prion disease is a fatal, incurable neurodegenerative disease of humans and other mammals caused by conversion of cellular prion protein (PrPc) into a self-propagating neurotoxic conformer (PrPSc). The most prevalent instance of prion disease, also known as human prion disease, is Creutzfeldt-Jakob disease (CJD). It is a rare, contagious neurodegenerative disorder involves epigenetic mechanisms such as DNA methylation, histone post-translational modifications, and microRNA-mediated post-transcriptional gene regulation. No proven cure for Creutzfeldt-Jakob disease is reported till date but clinical studies are under way at the National Prion Clinic (NPC) to investigate possible treatments. Treatment is constrained by symptomatic response due to unexplored underlying drug targets. Research trend shifted towards lowering PrPc expression as principal therapeutic strategy. Antisense oligonucleotides (ASOs) can offer a feasible means of reducing target mRNA in the brain to prolong the longevity of prion-infected species, according to in vivo studies as reported. Various Anti-Prion Systems have been developed in Saccharomyces cerevisiae by continuously working in the normal cell without overproducing or lacking any protein. These systems have negative effects on prions by blocking their formation, curing many prions after they arise, preventing prion infections, and lowering the cytotoxicity produced by prions. As several Anti-Prion Systems have been developed with a single microbial system as reported till date, future studies focusing on other microorganisms may also be taken into account to effectively establish this as a novel therapeutic strategy.
Keywords: Prion protein, Creutzfeldt-Jakob Disease, Anti-Prion System, Saccharomyces cerevisiae