{"id":200,"date":"2013-07-10T13:29:20","date_gmt":"2013-07-10T13:29:20","guid":{"rendered":"http:\/\/blogs.kent.ac.uk\/biosciences\/?p=200"},"modified":"2013-07-10T13:29:20","modified_gmt":"2013-07-10T13:29:20","slug":"new-insights-into-what-makes-prions-infectious","status":"publish","type":"post","link":"https:\/\/blogs.kent.ac.uk\/biosciences\/2013\/07\/10\/new-insights-into-what-makes-prions-infectious\/","title":{"rendered":"New insights into what makes prions infectious"},"content":{"rendered":"

\"Figure<\/a>Prions are a remarkable type of disease-causing agent being entirely composed of protein. Nevertheless they are able to replicate themselves once in their host but understanding how they do so remains a major challenge. In a recent study published by Mick Tuite and his former PhD student Ricardo Marchante, the importance of so-called conformational flexibility of the prion protein has been identified as major factor in directing prion replication. Their studies on yeast prions, published in the June 6th<\/sup> issue of Molecular Cell, identify mutations in a yeast prion that impede replication by constraining the necessary flexibility of the prion protein.<\/p>\n

Paper: Marchante, R.M.N., Rowe, M., Zenthon, Howard, M.J. and Tuite, M.F<\/b>. (2013) Structural definition is important for the propagation of the yeast [PSI<\/i>+<\/sup>] prion. Molecular Cell<\/i> 50:<\/b> 675\u2013685.<\/p>\n