Soil Mineral Degrades the Nearly Indestructible Prion
Posted on January 15, 2009 Comments (3)
Warped pathogens that lack both DNA and RNA, prions are believed to cause such fatal brain ailments as chronic wasting disease (CWD) in deer and moose, mad cow disease in cattle, scrapie in sheep and Creutzfeldt-Jakob disease in humans. In addition to being perhaps the weirdest infectious agent know to science, the prion is also the most durable. It resists almost every method of destruction from fire and ionizing radiation to chemical disinfectants and autoclaving, which reduce prion infectivity but fail to completely eliminate it.
Other studies have shown that prions can survive in the soil for at least three years, and that soil is a plausible route of transmission for some animals, says Joel Pedersen, a UW-Madison environmental chemist. “We know that environmental contamination occurs in deer and sheep at least,” he notes.
Prion reservoirs in the soil, Pedersen explains, are likely critical links in the chain of infection because the agent does not appear to depend on vectors — intermediate organisms like mosquitoes or ticks — to spread from animal to animal.
That the birnessite family of minerals possessed the capacity to degrade prions was a surprise, Pedersen says. Manganese oxides like birnessite are commonly used in such things as batteries and are among the most potent oxidants occurring naturally in soils, capable of chemically transforming a substance by adding oxygen atoms and stripping away electrons. The mineral is most abundant in soils that are seasonally waterlogged or poorly drained.
Related: Clues to Prion Infectivity – Scientists Knock-out Prion Gene in Cows – Curious Cat Science and Engineering Search
Categories: Life Science, Research, Science, Students
Tags: Life Science, Madison, prion, university research
3 Responses to “Soil Mineral Degrades the Nearly Indestructible Prion”
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January 15th, 2009 @ 9:42 am
We hope this will lead to effective control of CWD in wild ungulates. In one location in Colorado all animals were removed from a prion infected site for seven years however when ungulates were reintroduced to the site they all became infected with CWD. More research needs to be done on this problem.
April 18th, 2010 @ 3:22 pm
“Alzheimer’s disease has long been linked to the build-up of amyloid-β peptides, first into relatively short chains known as oligomers, and then eventually into the long, sticky fibrils that form plaques in the brain…”
April 18th, 2010 @ 5:17 pm
Researchers at University of California, Santa Cruz, and other scientists, have declared that Alzheimer’s Disease (AD) is a prion disease – TSE – transmissible spongiform encephalopathy. http://www.sludgevictims.com/pathogens/ALZHEIMERS-CJD-samepriondisease.doc
Infectious prions have been found in human and animal muscle tissue, including heart and skeletal muscle.
“These in vitro studies also suggest that in vivo prion infection of skeletal muscle requires contact with prion-infected neurons or, possibly, nerve terminals.”
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1900159/?tool=pubmed
Prions have also been found in saliva, blood, urine, feces and many other organs of human and animal victims of TSEs.
“.In addition to the brain and other organs known to be prion positive in vCJD, such as the lymphoreticular system, pituitary and adrenal glands, and gastrointestinal tract, PrPres was also detected for the first time in the dura mater, liver, pancreas, kidney, ovary, uterus, and skin.”
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2808239/
This raises the issue of iatrogenic transmission of Alzheimer’s prion disease from infected blood and tissues, via medical, surgical, dental instruments, etc.
“These in vitro studies also suggest that in vivo prion infection of skeletal muscle requires contact with prion-infected neurons or, possibly, nerve terminals.”
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1900159/?tool=pubmed
Dr. Claudio Soto, et al, Univ. of Texas, and other researchers, have found prions in blood. “. . . whereas at the symptomatic phase, PrPSc in blood was more likely to have leaked from the brain” . . . “These findings represent the first time that PrP(Sc) has been detected biochemically in blood, offering promise for developing a noninvasive method for early diagnosis of prion diseases.” http://www.sciencemag.org/cgi/content/abstract/313/5783/92
Researchers at Stanford University are closing in on a blood test to identify AD before the appearance of symptoms . . . ”
http://alzheimers.about.com/lw/Health-Medicine/Geriatric-Health/Blood-Tests-for-Alzheimers-Disease-Diagnosis.htm
Recent science indicates blood-borne infections may exacerbate AD.
“The researchers suspect that the memory loss is related to a protein related to inflammation that circulates in the blood during an infection. ‘
http://www.livescience.com/health/090909-infection-alzheimers.html
“Some new evidence indicates that disruption of the blood-brain barrier in Alzheimer’s Disease patients allows blood plasma containing amyloid beta (Aβ) to enter the brain where the Aβ adheres preferentially to the surface of astrocytes. ”
” Thus, in some patients, Alzheimer’s disease may be caused (or more likely, aggravated) by a breakdown in the blood-brain barrier. [1] ”
http://en.wikipedia.org/wiki/Blood-brain_barrier#Alzheimer.27s_Disease
Recent science raises the issue of infectivity of protein misfolding disorders: Dr. Claudio Soto, et al
http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TCV-4J84SMK-1&_user=10&_coverDate=03%2F31%2F2006&_rdoc=1&_fmt=high&_orig=browse&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=8c46d0a95675da5acc91cd249f7e9071
Amyloids, prions and the inherent infectious nature of misfolded protein aggregates
“The molecular mechanism of prion conversion has a striking resemblance to the process of amyloid formation, suggesting that misfolded aggregates have an inherent ability to be transmissible. Intriguing recent data suggest that other protein misfolding disorders might also be transmitted by a prion-like infectious process’
Protein Misfolding Disorders… is Alzheimer’s Contagious?
September 23, 2006Posted by Hegemony in Health, Science.
“The best evidence for prion like activity in PMDs is in the case of systemic amyloidosis. In this disease an inflammatory response causes serum amyloid-A (SAA) protein to be deposited in various organs causing damage. This can be triggered in mice by eliciting an inflammatory response. The progression of the disease is increased dramatically with exposure to spleen or liver extract containing amyloid plaques. Additionally, study of mouse senile amyloidosis shows that oral administration of amyloid fibrils can cause the development of severe amyloid plaques.”
http://hegemony.wordpress.com/2006/09/23/protein-misfolding-diseases-is-alzheimers-contagious/
BLOOD-BORNE DISEASES -“Alzheimer’s disease and infection: do infectious agents contribute to progression of Alzheimer’s disease?”
“Infection with several important pathogens could constitute risk factors for cognitive impairment, dementia, and Alzheimer’s disease (AD) in particular. This review summarizes the data related to infectious agents that appear to have a relationship with AD. Infections with herpes simplex virus type 1, picornavirus, Borna disease virus, Chlamydia pneumoniae, Helicobacter pylori, and spirochete were reported to contribute to the pathophysiology of AD or to cognitive changes”
http://www.ncbi.nlm.nih.gov/pubmed/19560105?itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVAbstract
There are 5.3 million AD victims in the United States, with a new case every 70 seconds – an epidemic of almost a half million new cases of a transmissible prion disease each year. The CDC and medical community must promptly deal with the issue of potential iatrogenic transmission of Alzheimer’s Disease. With the potential for lawsuits, human lives, and millions of dollars worth of dental, medical and surgical equipment at risk, it is foolhardy to leave the question of iatrogenic transmission of AD unanswered.