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From: TSS ()
Subject: UTMB researcher finds key to mad cow disease
Date: May 4, 2005 at 8:29 am PST

-------- Original Message --------
Subject: UTMB researcher finds key to mad cow disease
Date: Wed, 4 May 2005 10:09:08 -0500
From: "Terry S. Singeltary Sr."
Reply-To: Bovine Spongiform Encephalopathy

##################### Bovine Spongiform Encephalopathy #####################

UTMB researcher finds key to mad cow disease

By Nathan Smith

The Daily News

Published May 4, 2005

GALVESTON — Worry about mad cow disease may have dwindled among
consumers, but cattle ranchers worldwide remain painfully aware that
without a cure, the illness isn’t going away.

For decades, a theory has been debated in neuroscience circles that
degenerative illnesses such as mad cow disease, Scrapie and even
Alzheimer’s disease are caused not by viruses or bacteria but by a
malformed protein.

Dr. Claudio Soto, a professor of neurology at the University of Texas
Medical Branch, has spent the better part of his life studying the ways
certain kinds of proteins can ravage the brain. The doctor and his
research team say they have a made a breakthrough that has health care
professionals — and ranchers — the world over taking notice.

Currently, the only way to test cattle — and people — for diseases like
mad cow is to dissect the brain.

Soto and his team say their discoveries have led to an early testing
method for blood and food products that will help doctors detect the
presence of brain-destroying diseases before they can do much damage —
the first step in developing effective treatments.


Divide And Multiply

The diseases Soto studies start when brain cells begin producing
proteins in the wrong shape. These misshapen proteins would slowly
change the healthy shape of neighboring proteins in the brain, forming
clumps of sick proteins. Or so the theory went.

This hypothesis on transmissible misshapen proteins, or “prions,”
bending other proteins out of whack inside the brain was first proposed
in 1982. However, scientists were never able to prove it by growing the
infectious prions in a test tube and testing them on a lab animal.

Because it can take years for prions to damage enough healthy proteins
to be noticeable, producing a usable sample from a test tube would
ordinarily take decades.

In April, however, Soto’s team published a thesis in the journal Cell
revealing that they had developed a technique to rapidly speed up the
prion “misfolding” process by breaking up large strands of proteins
using bursts of ultrasonic waves.

By breaking a single sample into many, researchers can multiply the
number of microscopic growing samples hundreds of times over.

“That was the breakthrough,” Soto said. “For many years, people have
tried to make these infectious prions in test tubes, because what is
needed to prove the prion hypothesis completely is to be able to produce
this process in vitro in the absence of living cells and thus rule out
the presence of a virus.”

The problem, Soto said, had always been cultivating enough prions in a
test tube. Finally, he had his answer.

“The evidence in favor of the prion hypothesis was strong, but the final
proof was still missing,” he said. “Now we have supplied this proof.”

But Soto had not merely proven an interesting theory. Instead, he and
his team have opened the door to understanding some of the brain’s most
devastating diseases.

In creating a process in which prions can replicate quickly to
detectable levels, researchers built the foundations of a method to test
blood and food supplies for the presence of diseases such as mad cow and

Currently, such diseases are only detectable decades after the first
problems occur. By that time, it is too late.

“When people begin to develop symptoms of these diseases, more than 50
percent of the brain is already lost,” Soto said. “The next step is
using this technology to detect prions in the blood; that way we can
diagnose the disease before the damage occurs.”


Unknown Risk

Because there has previously been no way to test for them, millions of
gallons of blood in the world’s blood banks and a significant chunk of
the world’s beef supply could conceivably be infected without anyone
knowing it.

“No one knows how many people are infected, because the diseases’
incubation time is so long,” Soto said. “We can’t say there aren’t
100,000 people incubating, donating blood.”

Once the testing process is tried upon humans and animals, Soto hopes
that will change. Though some skepticism remains over the
long-controversial theory, many of Soto’s peers have already begun
considering the implications of his work.

“This is a major advance,” said Dr. Jonathan Weissman, a professor in
cellular molecular pharmacology at the University of California at San
Francisco and an investigator for the Howard Hughes Medical Institution.
“I think there are possibilities there for not only developing a much
more sensitive way of testing for prions, but a very nice tool for
seeing if blood or food is contaminated. In time, it could also be a
tool for looking for agents that could potentially block the process.”

In other words, to find a cure. But Soto says there is still much work
to be done before that can be accomplished.

“This is a very unique system by which diseases can be transmitted,” he
said. “How common is the prion method of transmitting information?”

Though the researcher might speak dispassionately about the subject of
his work, a twinkle in his eye reveals that he will have fun finding out.

“Our next step is to start working with human and animal samples,” Soto
said with a smile. “Nobody cares about diagnosing hamsters.”


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