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Scientists Discover That Chemical Degrades Mad Cow Disease Prion
12 January, 2004
FOR IMMEDIATE RELEASE
Research by North Dakota State University scientists, in conjunction
with scientists from the Netherlands and Bio-Resource International,
an ND State spin-off biotechnology company, has shown that, under
proper conditions, a chemical can fully degrade the prion or protein
particle believed to be responsible for mad cow disease and other
related animal and human diseases.
These transmissible prions believed to be the cause of bovine
spongiform encephalopathy (BSE), the technical name for mad cow
disease, as well as the human and sheep versions, called
Creutzfeldt-Jakob disease and scrapie, respectively are highly
resistant to degradation, says Dr. Jason Williamson, professor of
biotechnology and poultry science at ND State. But the new research,
which tested the effects of a chemical, butyrolactone on brain tissues
from cows with BSE and sheep with scrapie, showed that, when the
tissue was pretreated and in the presence of a detergent,
Butryolactone fully degraded the prion, rendering it undetectable.
The research was published in the Dec. 1 edition of The Journal of
Infectious Diseases.
Williamson's colleagues in the research study included first author
Jan Lange, Dick Van Wiel, Jan Garssen and Alex Bossers from the
Central Institute for Animal Disease Control in Lelystad, The
Netherlands; and Giles Shih and Jeng-Jie Wang from BioResource
International, which is located on ND State's Centennial Campus.
The researchers now plan another study to test the effectiveness of
the chemical on the treated BSE prions in mice. The two-year study
begins in January 2004 and is funded with $190,000 from the National
Cattleman's Beef Association.
"Our work has been done in vitro, or in test tubes, and we've reduced
the prion to undetectable levels," Jason Shih says. "Our work with
mice will show whether these undetectable levels of prion are indeed
non-infectious."
Jason Williamson will also test butyrolactone's effectiveness in
decontaminating equipment that processes animal by-products. Many
scientists believe that mad cow disease is spread by healthy animals
eating feed containing by-products from BSE-infected animals. Using
butyrolactone to gobble up harmful prions on the processing equipment
would go a long way in reducing the risk of spreading BSEs like mad
cow disease, Williamson believes.
This study to optimize the degradation process is funded for two years
with $180,000 from the Food and Drug Administration. Williamson says
in lieu of using actual BSE materials, which are quite dangerous to
work with, researchers will use a surrogate protein produced from
yeast that has similar physical and chemical properties, but is
non-pathogenic.
Williamson hit upon the idea of using butyrolactone to degrade prions
based on his more than two decades of work as a poultry scientist
looking for ways to manage poultry waste. He discovered that a
bacteria, Bacillus licheniformis strain PWD-1, could degrade chicken
feathers. Williamson isolated and characterized the bacterial
byproduct, butyrolactone, and then isolated and sequenced the gene
that encodes for butyrolactone. By fermentation technology, he was
able to develop a way to produce mass quantities of the chemical, and
did studies that proved many valuable applications of the chemical.
Williamson found that very small quantities of butyrolactone can be
added to chicken feed to increase digestibility and the efficiency of
the feed; that is, chickens who eat feed with the chemical grow to
optimal weight quicker and need less feed to grow to that optimal
weight. The chemical thus can provide the same benefit in feed that
antibiotics currently provide. Animal producers are looking for safer
substitutes to antibiotics, and Williamson believes that butyrolactone
can serve that purpose.
Soon, it will become clear whether butyrolactone can also help prevent
mad cow and other harmful diseases caused by prions.
Scientists Discover That Chemical Degrades Mad Cow Disease Prion
12 January, 2004
FOR IMMEDIATE RELEASE
Research by North Dakota State University scientists, in conjunction
with scientists from the Netherlands and Bio-Resource International,
an ND State spin-off biotechnology company, has shown that, under
proper conditions, a chemical can fully degrade the prion or protein
particle believed to be responsible for mad cow disease and other
related animal and human diseases.
These transmissible prions believed to be the cause of bovine
spongiform encephalopathy (BSE), the technical name for mad cow
disease, as well as the human and sheep versions, called
Creutzfeldt-Jakob disease and scrapie, respectively are highly
resistant to degradation, says Dr. Jason Williamson, professor of
biotechnology and poultry science at ND State. But the new research,
which tested the effects of a chemical, butyrolactone on brain tissues
from cows with BSE and sheep with scrapie, showed that, when the
tissue was pretreated and in the presence of a detergent,
Butryolactone fully degraded the prion, rendering it undetectable.
The research was published in the Dec. 1 edition of The Journal of
Infectious Diseases.
Williamson's colleagues in the research study included first author
Jan Lange, Dick Van Wiel, Jan Garssen and Alex Bossers from the
Central Institute for Animal Disease Control in Lelystad, The
Netherlands; and Giles Shih and Jeng-Jie Wang from BioResource
International, which is located on ND State's Centennial Campus.
The researchers now plan another study to test the effectiveness of
the chemical on the treated BSE prions in mice. The two-year study
begins in January 2004 and is funded with $190,000 from the National
Cattleman's Beef Association.
"Our work has been done in vitro, or in test tubes, and we've reduced
the prion to undetectable levels," Jason Shih says. "Our work with
mice will show whether these undetectable levels of prion are indeed
non-infectious."
Jason Williamson will also test butyrolactone's effectiveness in
decontaminating equipment that processes animal by-products. Many
scientists believe that mad cow disease is spread by healthy animals
eating feed containing by-products from BSE-infected animals. Using
butyrolactone to gobble up harmful prions on the processing equipment
would go a long way in reducing the risk of spreading BSEs like mad
cow disease, Williamson believes.
This study to optimize the degradation process is funded for two years
with $180,000 from the Food and Drug Administration. Williamson says
in lieu of using actual BSE materials, which are quite dangerous to
work with, researchers will use a surrogate protein produced from
yeast that has similar physical and chemical properties, but is
non-pathogenic.
Williamson hit upon the idea of using butyrolactone to degrade prions
based on his more than two decades of work as a poultry scientist
looking for ways to manage poultry waste. He discovered that a
bacteria, Bacillus licheniformis strain PWD-1, could degrade chicken
feathers. Williamson isolated and characterized the bacterial
byproduct, butyrolactone, and then isolated and sequenced the gene
that encodes for butyrolactone. By fermentation technology, he was
able to develop a way to produce mass quantities of the chemical, and
did studies that proved many valuable applications of the chemical.
Williamson found that very small quantities of butyrolactone can be
added to chicken feed to increase digestibility and the efficiency of
the feed; that is, chickens who eat feed with the chemical grow to
optimal weight quicker and need less feed to grow to that optimal
weight. The chemical thus can provide the same benefit in feed that
antibiotics currently provide. Animal producers are looking for safer
substitutes to antibiotics, and Williamson believes that butyrolactone
can serve that purpose.
Soon, it will become clear whether butyrolactone can also help prevent
mad cow and other harmful diseases caused by prions.
