Scientists at the University of Liverpool have determined the atomic structure of the 'binding' between a brain protein and an antibody that could be key to treating patients with diseases such as variant CJD.
Variant Creutzfeldt-Jakob Disease (vCJD) is part of a family of rare progressive neurodegenerative disorders, called prion diseases, which affect both animals and humans. It is thought that those who have developed vCJD became infected through the consumption of cattle products contaminated with Bovine Spongiform Encephalopathy (BSE) - a brain disorder in cows, commonly known as Mad Cow Disease.
Prion diseases can develop when a naturally occurring brain prion protein called, PrP, comes into contact with infectious prions. This converts PrP into a form that has a different shape, and eventually leads to a build-up of protein in the brain, causing brain cells to die. It is thought that immunisation with antibodies that can 'stick' to PrP could treat and even prevent the development of the disease.
To understand the 'connection' between the antibody and the protein, scientists at Liverpool used X-ray crystallography technology to build a three-dimensional picture of the binding between an antibody called ICSM18 - designed to 'stick' effectively to prion proteins - and PrP cells.