Registration for a live webinar on 'Gamma-delta T cells for immunotherapy of cancer' is now open.See webinar details
Chaperones and prions
A selection of talks on Biochemistry
The ERK1/2 MAPK cascade
- Prof. Melanie H. Cobb
- University of Texas Southwestern Medical Center at Dallas, USA
Amino acid conjugation: mechanism and enzymology
- Dr. Kathleen Knights
- Flinders University, Australia
Hello, my name is Yury Chernoff. I'm a professor at Georgia Institute of Technology, located in Atlanta, United States. Today, I'm going to talk about chaperones and prions.
Prions were initially described as infectious agents which cause neurodegenerative diseases in humans and in other mammals. One example of such a disease is 'mad cow disease', which can be transmitted from cows to humans. Prion diseases are usually fatal and incurable diseases, therefore they represent a significant problem for the animal breeding industry and for human health.
Perhaps the most interesting feature of prion diseases is an unusual mechanism of transmission. The prion infectious agent is composed of a protein in an abnormal shape. In the process of infection, the prion protein converts a non-prion host protein of the same amino acid sequence into a prion. Prion proteins form fiber-like aggregates enriched in beta-structures and cause amyloid. Recent models suggest that prion propagation represents a process of amyloid nucleated polymerization. In this way, prions resemble the other amyloid diseases and so-called 'neural inclusion disorders' such as Huntington's disease, Alzheimer's disease, and many others.