Thursday, August 26, 2021 30-Year NIAID Project Reveals Structures of Infectious Prions For comparison, the normal form of the prion protein is shown tethered to a cell membrane beside the corrupted form that is infectious. This graphic image was created after scientists analyzed thousands of data points from images collected of the infectious prions. After 30 years of steady progress, NIAID scientists and colleagues from Case Western Reserve University in Cleveland have solved the structure of an infectious prion protein and have created 3D images of their model. Their work, published in Molecular Cell, will help researchers better understand the changes that take place when normal prion protein converts to an infectious prion form. They believe this understanding will allow scientists to target steps where treatment might be effective at slowing or preventing the spread of disease. But, like the lengthy project to identify the structure, using the model to develop clinical applications may be years away. National Institute of Allergy and Infectious Diseases  |  National Institutes of Health Update your subscriptions, modify your password or e-mail address, or stop subscriptions at any time on your Subscriber Preferences Page. You will need to use your e-mail address to log in. If you have questions or problems with the subscription service, please contact Subscriber Help. This service is provided to you at no charge by National Institute of Allergy and Infectious Diseases (NIAID).                             This email was sent to myhcistech.healthnews360@blogger.com using GovDelivery Communications Cloud on behalf of: National Institute of Allergy and Infectious Diseases · 5601 Fishers Lane · Bethesda, MD 20892 · 1-866-284-4107