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Deadly game: chronic wasting disease


October 27, 2002 Milwaukee Journal Sentinel by John Fauber And Mark 
Johnson Jfauber@Journalsentinel.Com

At 2 a.m. on Aug. 10, a hearse carrying the hollowed, 50-pound body of Alice Dumas left Beloit, bound for the pathology department at the University of Wisconsin Hospital in Madison.

Normally, undertakers take bodies away from hospitals; Alice, a once-beautiful mother of two, was headed in the opposite direction.

Something rare appeared to have killed her -- Creutzfeldt-Jakob disease, which strikes one in a million people, eroding the brain and causing the body to waste away. Rarer still was her age: 44. The majority of victims are about a quarter-century older. To be sure of Alice's killer, doctors in Madison needed to search sections of her brain for signs of an unusual and menacing infectious agent. When they finished, her tissue was packed on dry ice and flown to a laboratory in Cleveland for more testing. Scientists there took special care to protect themselves, wearing bioprotective suits and three pairs of gloves each.

Almost daily, brain tissue from Creutzfeldt-Jakob patients across the country arrives by Federal Express at the Cleveland lab.

In a way, the lab is America's sentry, watching for the frightening possibility that a human may have contracted the terrible disease from an animal. The sample from Alice's brain joined many others, including samples from a handful of outdoorsmen from Wisconsin and other states who also died of the disease.

Understanding how Alice, who never hunted a day in her life, and the outdoorsmen, who feasted on venison, ended up with Creutzfeldt-Jakob is part of a larger scientific quest to explain a strange family of diseases. That quest gained urgency this year as a close relative of Creutzfeldt-Jakob, chronic wasting disease, crossed the Mississippi River for the first time, infecting Wisconsin's white-tailed deer herd.

Both diseases are believed to be caused by the same deadly agent, a mutant protein called a prion.

The prion is a new kind of killer. Devoid of genetic material, it's neither virus nor bacterium. Instead, this rogue agent does its dirty work by taking root in otherwise healthy brains, destroying cells and leaving behind a grim calling card: spongelike holes.

Prions are highly infectious and notoriously difficult to destroy, which is why the scientists in Cleveland went to such lengths to ensure that their skin never touched the tissue from Alice's brain.

But these microscopic molecules also have proved elusive and controversial; scientists have yet to isolate a single one, and skeptics doubt they ever will.

This much is known: This mysterious agent can cross the biological barrier from one species to another.

In the 1990s, a prion disorder called mad cow disease jumped from cattle to humans, appearing as variant Creutzfeldt-Jakob disease and killing about 130 young beefeaters so far, most of them in Great Britain. Because the disease can incubate for years and possibly decades, estimates of the ultimate human toll from mad cow vary wildly, from a few hundred to more than 100,000.

"The question is: Does wasting disease go to humans?" said Al Anderson, assistant professor of neurology at the University of Colorado, who is now tracking unusual brain diseases among Coloradans who hunt, raise, butcher or consume wild game.

No human has yet been found to be infected with chronic wasting disease. But the British experience with mad cow -- and especially the early government line that the disease posed no threat to people -- has loomed large in the minds of North Americans studying chronic wasting disease.

Researchers find themselves asked more and more whether it is safe to eat venison.

"I have struggled and wrestled with this question," said Gregory Poland, who is a professor of medicine at Mayo Medical School and also hunts deer in Minnesota, the latest state where chronic wasting disease has been found. "The awful truth is there is not a clear answer right now, because we simply don't know. It is biologic Russian roulette."

Beyond the immediate concern about meat, chronic wasting disease has intensified the work of scientists seeking to learn more about prion diseases and other neurological disorders.

The brains of Alice and the outdoorsmen could unlock secrets, not only about rare brain diseases such as Creutzfeldt-Jakob, but about more common human afflictions, including Alzheimer's disease and Parkinson's disease. Misfolded proteins appear to play a role in all of these ailments.

An agonizing descent Siblings puzzled by erratic behavior

Exactly how the deadly molecules entered Alice's brain remains a mystery.

"It's got to be something in the environment," said her older sister, Virgie Tipler. "Alice didn't eat deer, and she didn't go out of the United States. If she ate (venison), she didn't know she was eating it."

Once inside her, the disease took its time. More than 85% of people with the most common form of Creutzfeldt-Jakob disease die within a year, although the illness can be as short as one month and as long as six years.

With Alice, the agonizing decline began around 1997, five years before her death. One day she reported to her job assembling windows in a Beloit factory and began putting them together -- backward. She was fired soon afterward.

Her next position was with a temporary employment company. When she started showing up at the wrong work sites, she lost that job.

Three years ago, a relative got her a job cleaning restrooms. After she finished a restroom, she would walk out, then return to the same room and start cleaning it again.

Alice often repeated herself to family members. She forgot things: her children's birthdays; how to sit down for meals; how to get to her sister's home three blocks away.

In one incident, she worried she had lost her grandchild at the store and had everyone look for him. It turned out Alice had never taken him to the store. The boy was home with his great-grandmother.

She began to walk tentatively, taking baby steps, needing to clutch someone for balance.

Alice's relatives were puzzled. One sister thought she might have a brain tumor. Another thought she might have early Alzheimer's disease, even though there was no family history of the disorder. Still another sister wondered if it was related to her past use of cocaine, a habit she had stopped in 1991 when she became a regular churchgoer.

On the outside, it was the same petite Alice who jokingly boasted, "I'm so fine, I'm so fine."

But Alice's brain was not fine.

Lethal and resilient Scientists document different prion diseases

Although the term prion was coined only 20 years ago, doctors have known for years about some of the diseases it causes.

Named for its discoverers, Creutzfeldt-Jakob disease first was described in 1920 and '21 by two German neuropsychiatrists working independently.

There are three types: genetic, sporadic and acquired.

The last is the rarest, and involves some 250 documented cases of people worldwide who developed Creutzfeldt-Jakob disease after undergoing medical procedures such as injections of human growth hormone from cadavers, transplants of infected brain and corneal tissue and use of neurological instruments that were not properly sanitized.

The genetic version accounts for less than 15% of Creutzfeldt-Jakob cases; it is caused by a mutation that affects production of a normal brain protein.

The sporadic version accounts for the remaining 85% of cases; its cause is unknown.

In the 1950s, D. Carleton Gajdusek, an American research scientist, traveled to Papua New Guinea to study a disease called kuru that infected as many as 2,500 natives in the highlands. Gajdusek found that the disease spread through ritualistic cannibalism, as participants, usually women and children, ate highly infectious brains and other body parts from deceased relatives.

His pioneering work would later win a Nobel Prize and inspire others to study the strange family of diseases known as transmissible spongiform encephalopathies.

The 1980s brought another research milestone -- this one at Case Western Reserve University in Cleveland, the same school that would one day receive Alice's brain sample. A researcher named Pierluigi Gambetti was intrigued by a brain belonging to an Italian man whose descendants had been cursed by a bizarre neurological ailment, dating back to the 1700s. Marked by progressing dementia and insomnia, the disease caused victims to slowly waste away.

The patients burned calories normally conserved during sleep.

"Their bodies became like a racing engine," Gambetti said.

Denied the ability to sleep, they daydreamed until dreams and reality became indistinguishable. Then they died.

For Gambetti, a neuropathologist, unraveling the mystery of that illness would become a scientific epiphany.

"I was really determined to find out what was going on," he said.

Over the next several years, Gambetti and Elio Lugaresi, his former professor in Bologna, would identify a genetic form of Creutzfeldt-Jakob disease, a mutation in which the body essentially made its own prions. They named this genetic form "fatal familial insomnia." The disease since has been identified in families throughout the world, though the odds of developing it are a minuscule one in 33 million.

Whatever the disease, one factor remains constant: Prions are both lethal and resilient.

Unlike bacteria, they are highly resistant to heat and conventional sterilization methods. It takes temperatures as high as 1,080 degrees Fahrenheit to destroy them. Prions even have shown the ability to lurk in soil for years, infecting and killing otherwise healthy animals that ingest them while grazing.

"They're practically indestructible," said G. Richard Olds, professor of medicine at the Medical College of Wisconsin.

The human body appears to be no match.

Fading quickly Hospital tests point to rare, deadly disease

On an unusually warm March afternoon this year, two of Alice's sisters and a brother-in-law drove her to the UW Hospital in Madison.

Her sister Virgie Tipler was optimistic. Finally, the proper specialists would examine Alice.

"I really thought they could give her some medication, and she would be fine and we could bring her home," Tipler said later.

Instead, after more than a week of testing, a doctor mentioned that Alice might have a disease Tipler had never heard of: Creutzfeldt-Jakob.

"He said it was deadly," Tipler said. "He said if that is what it is, she won't have long."

After slowly brewing in Alice for years, the disease went on a rampage.

"Unfortunately, Ms. Dumas deteriorated with remarkable speed during her (four-week) hospitalization," a doctor wrote at her discharge. "Initially she was capable of some interaction. . . . By the end, her neurological exam was remarkable for the absence of any verbalization."

She was discharged on April 19 with a prescription for lorazepam, a tranquilizing, anti-anxiety drug, and the instruction to medical personnel "DNR," do not resuscitate.

Limited monitoring Researcher wants comprehensive effort

Maverick scientist Stanley Prusiner of the University of California at San Francisco first coined the term prion and prevailed over enough doubts about his theory to win the Nobel Prize. Still, some scientists suspected something else was causing diseases such as Creutzfeldt-Jakob and chronic wasting, perhaps a slow-acting, undetected virus.

Even those who work with Prusiner have conceded that they don't know exactly how prions infect normal tissue and convert it to the mutant form. They now say prions may contain another ingredient besides a lone protein molecule.

They call the mystery ingredient Protein X and suspect it is another protein that helps the prion trigger the destruction in the brain.

A few scientists, however, say such revisions cast doubt on the whole prion theory.

"The data for prions has crumbled," said Laura Manuelidis, head of neuropathology at Yale Medical School. "Protein X sounds a lot like a virus."

Whatever it is, the agent in Creutzfeldt-Jakob can linger in a person for years, even decades, before producing noticeable symptoms. In June, a British medical journal reported on what may be the longest incubation period: a man who developed Creutzfeldt-Jakob disease 38 years after undergoing a medical procedure.

The long incubation periods mean that if chronic wasting disease does cross the species barrier to humans, it may be years before doctors see the evidence: more people dying of some type of Creutzfeldt-Jakob after contact with deer.

So far, there has been no unusual jump in Creutzfeldt-Jakob cases in Colorado and Wyoming, where chronic wasting disease has existed for decades, although in sparsely populated areas.

In Wisconsin, there were 43 known Creutzfeldt-Jakob deaths between 1991 and 2000, according to death certificate information compiled by the state Division of Public Health. That's slightly less than one per million a year.

Nationwide reporting of the disease isn't mandatory, but a study in 2000 looked at Creutzfeldt-Jakob deaths between 1979 and 1998 and found an annual incidence of about one in every 1 million people.

The requirements for monitoring Creutzfeldt-Jakob disease aren't adequate, according to Gambetti, who directs the National Prion Disease Pathology Surveillance Center at Case Western Reserve. Last year, his lab received brain tissue samples from only half the Creutzfeldt-Jakob cases in the U.S., even though it is supposed to receive samples from all of them.

"It's a big problem," Gambetti said. "I could miss a variant CJD (the human version of mad cow) case."

Even with the incomplete monitoring, Gambetti said, a couple of disturbing trends might be developing.

"What I'm seeing is more younger cases, which was unheard of before," he said, referring to people in their 20s and 30s.

He's also noticed a rise in atypical forms of the sporadic disease.

Alice's brain sample was one of about 300 such packages expected to arrive this year at Gambetti's fourth-floor suite of labs and offices.

Other samples included tissue from three outdoorsmen who shared wild game feasts at a cabin on Wisconsin's Brule River and subsequently died of brain diseases. Their cases, first reported in the Journal Sentinel in July, are under investigation by the federal Centers for Disease Control and Prevention and the state Division of Public Health.

As part of its testing, the Cleveland lab will look for evidence of any brain disease that might have come from animals such as cattle infected with mad cow disease or deer infected with chronic wasting disease.

In its five years of operation, the lab has yet to find such a case.

Other labs have been looking for these cases, too. After mad cow disease jumped to humans, the Mayo Clinic re-examined all 158 cases of Creutzfeldt-Jakob it had recorded between 1976 and 1996, looking for anything atypical, and especially anything that looked like the human version of mad cow. Mayo, too, found nothing unusual.

Dying at home Doctor tries to help family as well

On a warm June day, in the living room of a Beloit home, physician Kenneth Gold leaned over Alice's bed and placed a stethoscope to her chest.

Her heart rate was fast, 123 beats a minute. Normal is 60 to 90. She had a temperature of 103 degrees. Most likely an infection, possibly pneumonia.

Family members looked in on Alice. Pictures of her grandson and longtime boyfriend hung on the wall above her.

"This is the way death used to be 100 years ago," Gold said. People died at home without artificial measures such as feeding tubes and respirators.

Like most doctors, Gold had little experience with Alice's ailment. Even if he had more, there's little he could have done. He was there as much for the family, whom he had known for more than 30 years, as he was for Alice herself.

"They need to be able to start grieving while she is still alive," Gold said.

Assessing risk Disease from deer might be hard to detect

While Creutzfeldt-Jakob disease remains unfamiliar to many family doctors, scientists know its signature, and they have learned the unique signature for human cases of mad cow disease as well.

But they're at a distinct disadvantage with chronic wasting disease. The fact that mad cow jumped to humans doesn't mean chronic wasting will. Scrapie, a prion disease in sheep, has not been shown to infect people.

And if chronic wasting disease does cross to humans, it might appear as a new kind of Creutzfeldt-Jakob disease, something scientists haven't seen before.

"It's difficult when you're watching for something and you're not sure what it will look like," said Anderson, the Colorado physician tracking Creutzfeldt-Jakob and other unusual brain diseases.

Doctors won't have an easy time proving that a human got sick from chronic wasting disease. They'll need evidence that the patient had substantial contact with deer or elk, and they'll have to rule out all other explanations for the disease, Anderson said. "I think, at best, it's going to be a circumstantial case."

The case for chronic wasting disease in humans could begin with a rise in the number of younger people contracting Creutzfeldt-Jakob, a sign that might point to a common source of infection, such as tainted meat.

In Europe, the median age of death for the more than 130 people who died from variant Creutzfeldt-Jakob was 28. In Wisconsin, the Division of Public Health has been tracking cases of Creutzfeldt-Jakob disease in people younger than 55.

Gambetti said he would like to see an additional measure across the U.S. All deer hunters who die of Creutzfeldt-Jakob disease, he said, should have the tonsils, spleen and lymph nodes removed and examined for evidence of prions. In classic Creutzfeldt-Jakob, prions are not normally found in those organs. But in the human version of mad cow disease, prions have been found there.

"I want to cover all the bases," Gambetti said. "I don't want to miss it. We are willing to pay to get the autopsies done. I'm willing to go there myself if I have to."

There are other reasons to closely monitor hunters and venison-eaters stricken with Creutzfeldt-Jakob disease. A small Temple University study in 1986 found that exposure to deer through a hobby such as hunting increased a person's risk of getting Creutzfeldt-Jakob by as much as ninefold.

Patrick Bosque, a Denver neurologist and prion researcher, said he believes the risk of chronic wasting disease jumping to people is being underplayed. Although humans don't appear to be "highly susceptible" to chronic wasting disease, Bosque said research suggests they may be as susceptible to the disease as they are to mad cow.

Bosque said that in his lab, when researchers work with mice exposed to prions, they wear gloves and hoods, and cannot bring in food, apply lip balm, even adjust their contact lenses.

"When I see pictures of people dressing deer in the field, there's just a huge difference in the level of biosafety," said Bosque, who worked with Prusiner and is now an assistant professor at the University of Colorado.

In a recent paper, Bosque concluded that "practical measures to limit human exposure to animal prions, particularly CWD-infected deer and elk, should be improved."

To avoid possible exposure to chronic wasting disease, hunters have been told not to eat any meat from infected animals, but the standard chronic wasting disease test, which examines tissue from the deer's brainstem, can be up to 30% inaccurate.

Hunters also have been told not to eat deer organs that prions infect, including the brain, spinal cord, eyes, spleen and lymph nodes.

The popular perception is that prions are not found outside of those tissues.

But new studies have found evidence that prions can exist in the muscle tissue of laboratory mice and in the blood of sheep.

Researchers say any prions in the blood of diseased deer probably exist at extremely low levels.

Still, the research "raises an obvious concern," said Judd Aiken, a UW associate professor of animal health and biomedical sciences. "If one wants to be safe, you would not consume any venison" from the area southwest of Madison where infected deer were first found.

This month, the Medical Society of Milwaukee County recommended that the state adopt the same regulations for deer processing that the British government imposed on its beef industry. The concern is that butchering venison and other meat in the same place with the same tools might pose risks.

Living on fluids Family goal is death with dignity

For the last five months of her life, Alice's family kept her alive by feeding her fluids mixed in a blender, gently coaxing her to swallow. They used foods such as Carnation Instant Breakfast, Ensure and blended baby food.

"She loved the Ocean Spray white cranberry juice," Tipler said.

She never left her bed.

Alice was always a petite woman. She was not quite 5 feet tall and never weighed more than 102 pounds. But by early August, she was a contorted shell of her former self. Bones bulged under her papery skin.

Her family felt the dignified way for her to die was without the aid of a feeding tube.

Biology gone awry Several diseases have common denominator

The downward spiral that brought Alice to this point began with subtle molecular changes in her brain.

Humans and animals have evolved to produce thousands of complex proteins within their cells, including one called prion protein. To carry out their functions, all proteins must fold into specific three-dimensional shapes. When a protein misfolds, it can have grave consequences.

Infectious prions and normal prion protein are chemically identical. Both are made up of more than 200 amino acids linked together in a chain.

But prions are misfolded in sections, taking on a flat shape rather than the normal spiraling pattern. Imagine a telephone cord pulled tight. Scientists believe these flat, uncoiled sections make prions lethal to brain cells.

In the brain, misfolded prions cause normal protein to uncoil, triggering a cascade of misfolding. All of this abnormal protein sticks together in clumps.

As the clumps build up, brain cells die. In humans, the death of these cells leads to memory loss, confusion and the inability to walk and swallow.

The process bears a striking similarity to what takes place in more common brain disorders such as Alzheimer's disease, Parkinson's disease and ALS (amyotrophic lateral sclerosis, or Lou Gehrig's disease). Those disorders also involve misfolded proteins that clump, eventually leading to the death of brain cells.

The similarities between the prion diseases and other brain disorders may mean that Alice's illness isn't the one-in-a-million rarity that doctors think. Small studies by the University of Pittsburgh Medical School and Yale University School of Medicine suggest that some people diagnosed with Alzheimer's and other forms of dementia might actually be dying from Creutzfeldt-Jakob disease.

The Pittsburgh study looked at autopsies from 54 patients thought to have died from other disorders and found that 5.5% had Creutzfeldt-Jakob. The Yale study of 46 people diagnosed with suspected Alzheimer's found that 13% turned out to have Creutzfeldt-Jakob.

The actual percentage of misdiagnosed cases is unlikely to be so high, but it could be up to 1%, said Oscar Lopez, associate professor of neurology at the University of Pittsburgh. Because an estimated 4 million Americans have Alzheimer's disease, a 1% rate of error would mean thousands of Americans, not hundreds, are dying of Creutzfeldt-Jakob.

Also, a growing number of scientists believe that understanding rare afflictions such as Creutzfeldt-Jakob might lead to cures for the more common diseases, such as Alzheimer's.

"Research for the rare diseases may have a huge impact," said Giuseppe Legname, a molecular biologist in Prusiner's lab. "If we understand how prions are made in cells, we might all of a sudden understand other diseases like Alzheimer's."

'I was relieved' Labored breathing, and then the end

It was a little past midnight, on Saturday, Aug. 10. Tipler sat beside Alice's bed, holding her sister's hand and reading the Bible to her.

Two days earlier, Alice had been semi-comatose. She seemed to wake up on Friday. But late Friday night, Tipler came downstairs to the living room, where her sister lay, and noticed that Alice's breathing was labored.

In the early minutes of Saturday morning, Tipler continued reading from the Book of John. She told Alice it was OK to pass on, it was OK for her to go home.

At 12:23 a.m., Alice's breathing stopped.

Undertakers from the Hansen Funeral Home arrived a short time later to take her body to the UW Hospital.

"It was best for her to go," Tipler said. "She had deteriorated from the inside out. I was relieved, but I was sorry. I was glad for her to stop suffering."

The Alice who once loved to play softball, ice skate, dance and get dressed up was gone.

"She was beautiful," Tipler said. "She smiled all the time."

Possible immunity? Amino acid structure might hold key

Scientists now are learning that some people have a genetic characteristic that may offer some resistance to prion diseases. This discovery could have implications for deer hunters and venison eaters who worry whether chronic wasting disease might infect people.

All of the variant Creutzfeldt-Jakob patients who were genetically tested had a similar amino acid structure for the normal prion protein in their bodies.

Normal prion protein is the same throughout humans, with a minor variation. At the 129th position in the chain, there are three possible combinations involving two different amino acids, methionine and valine.

Exactly which combination a person has depends on his parents. A methionine-methionine combination is found in about 40% of the European population. Every person who got mad cow disease had that combination. At least, that is what has been found in about 100 of the cases in which genetic analysis was done.

So far, no cases of variant Creutzfeldt-Jakob have been found in people with either of the other twopossible amino acid combinations. Could large numbers of people be blessed with the same genetic protection against chronic wasting disease?

"It's certainly possible," said Glenn Telling, associate professor and prion disease researcher at the University of Kentucky.

Telling is among a small group of researchers around the country who have created what are called transgenic mice. Those mice have a gene added that causes them to produce normal human prion protein in their brains.

Scientists use the mice because they cannot perform the ultimate test of chronic wasting disease's effect on people: injecting infected brain tissue directly into humans. The results of the mice studies probably won't be known for several months.

Researchers also are looking at potential treatments for prion diseases.

Scientists working with hamsters reported this year that the common antibiotic tetracycline appeared to disarm prions, making them vulnerable to digestion by an enzyme normally found in the brain.

And last year, scientists working with mouse brain cells found that the anti-malaria drug quinacrine and the anti-psychotic drug chlorpromazine interfered with the ability of prions to cause normal brain protein to misfold.

Gambetti, of the National Prion Disease Pathology Surveillance Center, said he believes a treatment or cure for human prion diseases will be found in the next five to eight years.

Others are less optimistic.

Because the diseases are rare, drug companies have less incentive to invest in prion research, said Peter Lansbury, an associate professor of neurology at Harvard Medical School.

"Anything that doesn't involve baldness, obesity or erections is a lot less attractive to the big pharmaceutical companies," Lansbury said. "They aren't going to open a lab into prion diseases."

A haunting question Two pictures, a hymn and a rose on the coffin

At noon on Aug. 14, 150 people filled the Church of Christ just across the state line in South Beloit, Ill., to pay their last respects to Alice.

Two pictures of an attractive woman sat on top of her casket as the mourners sang one of Alice's favorite songs, "Jesus Is Coming Soon."

"Troubles will soon be over Happy forever more When we meet on that shore Free from all care Rising up in the sky Telling this world goodbye"

After the service, a procession of cars made its way to Eastlawn Cemetery, on the north side of Beloit.

As family members and friends gathered around the grave site, Dorothy Crawford, Alice's sister, handed pink roses to several of Alice's grandchildren. The children placed the flowers on the nearby graves of relatives, including Alice's mother, who died in 2001. One of the children put a rose on Alice's coffin.

Six days later, Gold signed Alice's death certificate. The cause of death lists Creutzfeldt-Jakob disease, which does nothing to answer the one question that haunts Alice's family to this day:

How did she get it?

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