oddball interesting things 161223 Two New Tests 100% Accurate in Detecting Mad Cow, Creutzfeldt-Jackob Prions

POSTED BY: 1kiki
UPDATED: Saturday, December 24, 2016 23:24
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1KIKI

Saturday, December 24, 2016 10:02 AM

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The results, reported today in Science, could improve safety in blood banks and other medical facilities. This is especially true in the United Kingdom, where an estimated one in 2,000 people is an asymptomatic carrier of mad cow prions.

Wasn't the 'mad cow' risk from eating British beef supposed to be next to nothing? How long has science tried to find the answer while government pushed a false - but comforting and business-friendly - story?

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Two New Tests 100% Accurate in Detecting Mad Cow, Creutzfeldt-Jackob Prions

http://www.laboratoryequipment.com/news/2016/12/two-new-tests-100-accu
rate-detecting-mad-cow-creutzfeldt-jackob-prions

Prions are rogue proteins that can cause debilitating brain diseases in certain patients – and can be spread through surgeries or blood transfusions.

Two new tests report 100 percent accuracy in detecting cases of Creutzfeldt-Jakob (CJD) and mad cow disease (vCJD) – even at the earliest, presymptomatic stages.

The results, reported today in Science, could improve safety in blood banks and other medical facilities. This is especially true in the United Kingdom, where an estimated one in 2,000 people is an asymptomatic carrier of mad cow prions.

One test used protein misfolding cyclic amplification (PMCA), and identified 14 cases of vCJD among another 153 samples of blood from healthy patients. That work was led by doctors at the University of Texas Houston Medical School.

The second test combined PMCA with plasminogen-bead capture, and succeeded at the same 100 percent accuracy rate, picking out 18 mad-cow carriers from 256 plasma samples. Among those 18 were two who were at the very earliest stages of carrying the disease, without any symptoms at all. That work was led by a French team at the Université de Montpellier, among other institutions.

Together, the screening could eliminate a disease that doesn’t kill many – just several hundred over two decades globally – but which is uniquely devastating.

“Early diagnosis would allow any potential therapy to be given before substantial brain damage has occurred,” said Claudio Soto of the University of Texas, senior author of the first paper. “In the case of the blood supply, availability of a procedure to efficiently detect small quantities of the infectious agent would allow removal of blood units contaminated with prions, so that new cases can be minimized substantially.”

Prions, and the devastating diseases they cause, are still a relative mystery. Last year a team of scientists published a paper indicating that the “seeds” of Alzheimer’s and Creutzfeldt-Jakob could be transmitted by direct tissue contact, like that in brain surgery. Earlier research has indicated that brain-eating cannibals from Papua New Guinea were contracting a prion disease called kuru due to their traditional funerary banquets of the deceased.

1KIKI

Saturday, December 24, 2016 11:11 AM

How did your beloved 'democratic' party fuck up so badly?

SIGNYM

Saturday, December 24, 2016 11:24 PM

ANOTHER SPONGIFORM ENCEPHALOTPAHY TO WONDER ABOUT: DEER, ELK, MOOSE & CHRONIC WASTING DISEASE

Here is the latest:

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An infectious brain disease that has been killing deer, elk and moose both in the wild and on “captive farms” continues to stalk the land, expanding its domain to 23 states and two Canadian provinces since it was first identified in captive mule deer in a Colorado research facility in 1967.

Known as chronic wasting disease, or CWD, it has baffled scientists for decades. Where did it come from, and why is it spreading across the landscape? What health risks might it pose to humans who eat parts of infected animals? And can cattle get it from infected deer, elk, and moose, thus introducing it into the human food chain?
Elk with CWD

Cow elk with symptoms of chronic wasting disease. Credit: Dr. Terry Kreeger, Wyoming Game and Fish Department, and the Chronic Wasting Disease Alliance.

Recent research, primarily funded by the National Institutes of Health, has opened the door to one of the reasons this disease is so pervasive — and actually endemic in a large swath of land in northeastern Colorado and southeastern Wyoming.

According to researchers at The University of Texas Health Science Center at Houston (UTHealth), grass plants can bind, uptake and transport infectious prions. Why this is so important takes some understanding of what prions are.

Much smaller than bacteria, prions are single proteins that cannot be destroyed by typical “kill strategies” such as extreme heat or ultraviolet light.

“With prions, nothing like that works,” said Claudio Soto, Ph.D., a UTHealth researcher and lead author of an article about the topic published May 26, 2015, in Cell Reports.

These protein-based infectious agents cause the characteristic spongy degeneration of the brain, leading to emaciation, abnormal behavior, loss of bodily functions, and death. As such, they are responsible for a group of fatal diseases referred to as transmissible spongiform encephalopathy (TSE). The group includes so-called “mad cow disease” (bovine spongiform encephalopathy, or BSE) in cattle, scrapie in sheep, and variant Creutzfeldt-Jakob disease in humans, which, according to the World Health Organization, has been “strongly linked” to eating beef products contaminated with central nervous system tissue, such as spinal cord and brain, from cows infected with mad cow disease.

Soto’s team analyzed the retention of CWD and other infectious prion proteins and their infectivity in wheat grass roots and leaves that had been incubated with prion-contaminated material. They discovered that even highly diluted amounts of the material can bind to the roots and leaves. From there, they fed the wheat grass to hamsters, which became infected with the disease.

The team also found the infectious prion proteins in plants that had been exposed to urine and feces from prion-infected hamsters and deer.

In addition, the team found that plants can uptake prions from contaminated soil and transport them to different parts of the plant. By doing this, the plants can act as a carrier of CWD.

This means, Soto said, that plants may play an important role in environmental prion contamination and the horizontal transmission of the disease. (Horizontal transmission occurs when an infectious agent is transmitted between members of the same species.)

Scientists already knew that these CWD prions are good at binding to soil, especially clay-based soils, and that they can persist there. Soto said that when some of the soil where an infected dead animal had been buried was injected into research animals several years after it had been buried, the injected animals came down with prion disease.

The question then became: Can these prions bind to plants?

“Surprisingly, we found that they do bind to plants very efficiently,” he said. “Even more surprisingly, plants infected with the prions were able to transmit the disease when animals were fed the contaminated plants.”

Soto warns that there is a good possibilit

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