Latest Fungal prions Stories
By McDonnell, Gerald KEYWORDS Decontamination / Inactivation / Prion / Sterilisation Prion diseases present unique challenges to healthcare facilities, both in the care and treatment of patients.
Two Brown Medical School biologists have figured out the fate of healthy protein when it comes in contact with the infectious prion form in yeast: The protein converts to the prion form, rendering it infectious. In an instant, good protein goes bad.
The mysterious, highly infectious prions, which cause the severe destruction of the brain that characterizes "mad cow disease" and several human brain degenerative disorders, can be rendered harmless in the laboratory by a slight alternation of the three-dimensional conformation or shape of the prion protein's structure.
Amyloid fibers are best known as the plaque that gunks up neurons in people with neurodegenerative illnesses such as Alzheimer's and Creutzfeldt-Jacob disease--the human analog of mad cow disease. But even though amyloids are common and implicated in a host of conditions, researchers haven't been able to identify their precise molecular structures.
Howard Hughes Medical Institute researchers have provided the first detailed look at the core structure of the abnormal protein filaments found in at least 20 devastating diseases, ranging from Alzheimer's to Creutzfeldt-Jakob disease, the human version of â€œmad cowâ€ disease.