in 'mad cow disease' research
Source of Article: http://cordis.europa.eu/fetch?CALLER=EN_NEWS&ACTION=D&SESSION=&RCN=30538
Researchers at the UK's University of
Liverpool have discovered the atomic structure of the 'binding' between a
brain protein and an antibody that could be vital in the search for a cure
for neurodegenerative diseases such as variant CJD (Creutzfeldt-Jakob
Disease). Their findings are published in the Proceedings of the National
Academy of Sciences (PNAS).
Variant CJD has hit the headlines over the past two decades because of its
ability to transfer from cattle (where it causes the degenerative brain
disease Bovine Spongiform Encephalopathy (BSE), also known as 'mad cow
disease') to humans. It is a rare progressive neurodegenerative disorder that
humans can develop after eating beef products that are infected with BSE.
An unusual type of protein called a prion is
responsible for the development of variant CJD. Prions
can cause a range of illnesses known as TSEs
(Transmissible Spongiform Encephalopathies) which
include mad cow disease in cattle and scrapie in
Prion diseases are neurodegenerative conditions
that affect both animals and human beings. They develop when a natural brain
protein called PrP comes into contact with the
infectious prions. The prions
then transform the PrP proteins into a form with a
different shape which leads to a build-up of the protein in the brain,
causing brain cells to die. The scientists at Liverpool
are researching whether immunisation with certain
antibodies that would 'stick' to the PrP could
treat the disease and possibly even prevent its development.
To get a clearer picture of the connection between PrP
and antibodies, the scientists used X-ray crystallography technology. They
built a three-dimensional picture of how an antibody called ICSM18 would
stick to prion proteins and PrP
Samar Hasnain, Professor of Molecular Biophysics at
the University of Liverpool, said, 'To pinpoint where the antibody 'sticks'
to the protein we used X-ray crystallography, pioneered by Nobel Prize winner
Max Perutz. Significantly we found that the point at which the protein and
antibody came together was also where scientists at the Medical Research
Council (MRC) Prion Unit had identified a single
amino acid, which we now know has a significant impact on a patient's
susceptibility to prion disease.'
Scientists at the UK's MRC
Prion Unit at University College London
collaborated with the University
researchers. They found that not only could the ICSM18 antibody help prevent
brain cells from becoming infected with prions, but
it could also reverse early damage caused by the disease.
Professor John Collinge, Director of the MRC Prion Unit, said, 'We have shown that ICSM18 has the
highest therapeutic potential in animal and cell based studies, but we have
yet to establish its impact on people who have variant CJD or other prion diseases. We are currently working, however, to
make human versions of the antibodies for future trials in people.'
For more information, please visit:
University of Liverpool:
Medical Research Council (MRC):