Is Mad Cow Disease Caused by a Bacteria?

So there's no truth in the rumour that it is caused by Anonymous Posters, then?

Thanks so much for this info. An interesting study and relating the meningitis and TB relationships.

It asks more questions than it answers. To me this means it has opened a door to new possibilities.

I know of a farm that was tested Johne's free for decades, NEVER purchased cattle and as a stud, only sold stock. Used artificial insemination for breeding, so didn't bring even bulls onto property. A cow that was tested free multiple times finally returned positive. The poultry on that farm had "died off" a few years earlier, but had grazed the area where the poultry roamed (and defecated) ............. I wonder??

They now cannot sell any stock due to the Johne's classification.

A few of the other diseases also of interest.

Again, thanks for sharing.

It is common practice to incorporate chicken waste into cattle feed and vice versa, ....never did think that was a good idea...I hope this turns out to be the answer we have been searching for, for so long...

I've often wondered if feeding antibiotics to farm animals might close the door on some bacteria and open the door for others we were unaware of...this bug if it exists would I think be categorized as an extremophile due to its high heat tolerance...it is not destroyed through digestion and if an animal has it, it's also in his waste....

.."As a result of the first case of bovine spongiform encephalopathy (BSE) in the United States in December 2003, the Food and Drug Administration (FDA) temporarily banned the feeding of poultry litter to beef cattle. The temporary ban was put in place to allow the FDA time to assess the risks to human health associated with the practice. Ruminant protein was permitted to be fed to poultry at the time the temporary ban was put in place. Some scientists were concerned that the infectious agents of BSE could be passed to beef cattle via spilled feed or manure. Since that time, FDA has mandated the removal of all tissues that have been shown to carry infectious agents of BSE (i.e., specified risk materials) from poultry diets. As a result, the practical possibility of transmitting BSE to beef cattle via poultry litter was deemed to be zero by FDA. Poultry litter was again approved as a feedstuff for beef cattle in October 2005."...

https://extension2.missouri.edu/G2077

Chicken manure is also used extensively for fertilizer...

http://www.hgtv.com/outdoors/gardens/animals-and-wildlife/the-straight-poop-on-using-chicken-manure-as-fertilizer

..."The number of Americans living with Alzheimer's disease is growing — and growing fast. ... Of the estimated 5.5 million Americans living with Alzheimer's dementia in 2017, an estimated 5.3 million are age 65 and older and approximately 200,000 individuals are under age 65 and have younger-onset Alzheimer's."...

https://www.alz.org/facts/

"Eating beef from an animal infected with mad cow disease can lead to an untreatable condition that attacks the brain and is universally fatal, but symptoms can take decades to emerge. Thankfully, a new blood-screening technology can spot the condition, known as variant Creutzfeldt-Jakob disease, with 100 percent accuracy, perhaps years before it attacks.

Misfolded proteins called prions cause both mad cow and variant Creutzfeldt-Jakob disease. Once they invade the brain, they begin recruiting normal proteins and forcing them to adopt the same abnormal shape. The prions and the blighted proteins clump together forming increasingly large aggregate deposits that wreak havoc on the brain and invariably lead to death. The disease, however, has a long incubation period. “In the case of humans, the estimation goes from several years to a few decades,” says Claudio Soto, a neurologist at McGovern Medical School at UTHealth in Houston. “So it could be that you're exposed one day and then, 40 years after, you develop the disease.”

In the interim, the prions hang out in non-brain tissues such as the appendix and tonsils, and because they do not cause symptoms, the infected person becomes a silent carrier. Perhaps the worst outbreak of variant Creutzfeldt-Jakob disease occurred in the United Kingdom during the 1980s and 1990s, when large swaths of the population were exposed to beef contaminated with mad cow disease. Since then, there have been 277 cases in the U.K. and an epidemiological study published in 2013 estimates that another 1 in 2,000 people there, about 30,000 in total, are silent carriers. While it is not clear how many of these people will go on to develop the disease, blood donations from silent carriers could jeopardize the country’s blood supply, according to Soto. The new screening test stands to alleviate the uncertainty, however.

Soto led the team behind one of two studies published today in Science Translational Medicine that assessed a diagnostic test for variant Creutzfeldt-Jakob disease, which can detect very low levels of prion proteins in the blood.

Soto’s team and a team led by Daisy Bougard of the French Blood Establishment in Montpellier, France ran the test on blood samples from variant Creutzfeldt-Jakob disease patients in the U.K. and France. The two teams used slightly different methods, but the basic idea was the same: the test essentially mimics the progression of the disease in an accelerated, artificial environment. First the prion proteins are separated from the blood and combined with normal proteins, which take on an abnormal shape, forming aggregate clumps. Then, the aggregates are pulled apart and recombined with more normal proteins. The process is repeated over and over again, in effect replicating the prion proteins until very small quantities are amplified enough to be easily detected. If there are no prions present in the blood, nothing happens.

Between the two studies, the test was able to identify a total of 32 cases of variant Creutzfeldt-Jakob disease with 100% percent accuracy, and there were no false positives among the 391 controls, which included regular blood donors, patients with a different form of Creutzfeldt-Jakob disease, and patients with other neurological diseases. In addition, Bougard’s group was able to diagnose variant Creutzfeldt-Jakob disease in the blood of two patients 1.3 and 2.6 years before they developed clinical symptoms. The results not only confirm that the test can accurately diagnose the disease, but also suggest that it may be able make the diagnosis before patients develop symptoms, which could be particularly important in places like the U.K. with a large number of silent carriers. The test
will “improve the safety of our blood supply [by eliminating] any blood samples that may be potentially contaminated with prions,” says Soto, “which will in turn diminish the possibility of people getting infected, and eventually developing this fatal disease.”

Soto founded a startup called Amprion to develop the technology. The company is currently working on optimizing the test and obtaining approval in the United States and Europe to use it for blood screening. Soto expects it to be commercially available within one to two years.

Paul Brown, formerly a senior investigator in the Laboratory of Central Nervous System Studies at the National Institutes of Health, who was not involved in the studies praised the accuracy of the test, saying that the two papers “reflect the immense progress that testing has undergone during the past decade.” However, he pointed out that variant Creutzfeldt-Jakob disease is no longer a major global problem, with only two cases in 2016, and said the test would have been more useful during the peak of the epidemic.

Christina Orrú, a neurologist at the National Institutes of Health, who was not involved in the studies, thinks the test is still needed to screen and monitor prion contamination in the blood supply. “We currently don’t really understand the implications of silent carriers and if they could harbor another wave of variant Creutzfeldt-Jakob disease, particularly in the U.K.,” she says.

Sylvain Lehmann, a neurologist at France’s National Center for Scientific Research, who was not involved in the studies was also impressed by the sensitivity and specificity of the test, saying that the findings confirm that silent carriers can transmit the disease. Because the current versions of the test are complicated, labor-intensive and time consuming, they are not necessarily suitable for screening large volumes of blood, he says, but they could be useful for confirming a diagnosis, especially in silent carriers, or detecting variant Creutzfeldt-Jakob disease in at-risk patients who received a contaminated blood transfusion.

The test may also have other applications. Soto and Bougard point out that while variant Creutzfeldt-Jakob disease is rare, more common neurodegenerative disorders like Alzheimer’s and Parkinson’s are caused by a similar process of misfolded proteins aggregating in the brain and causing damage. Both are hopeful that the new test can be adapted to screen for these diseases at an early stage, before symptoms occur.

“This is a big problem with all these brain diseases, that when the disease manifests clinically, it's always very late, and at the time that the brain is largely destroyed,” says Soto. “We are trying to develop a blood test to detect Alzheimer's disease and Parkinson's disease before the clinical symptoms of the disease appear so we have better possibilities for therapies to work.”

Catherine Caruso

https://www.scientificamerican.com/article/new-test-spots-human-form-of-mad-cow-disease-with-100-percent-accuracy/

...begs the question is the presence of misfolded proteins already too late for treatment....If these diseases are caused by bacteria, detecting the presence of the bacteria and treating it may be preventative...

It could be that we have all been exposed, and the disease only progresses when the immune system is in a compromised state, and some people may have a natural immunity for some reason.....and others a propensity due to genetic characteristics....clearly infection does not affect everybody the same...nor does it progress in a uniform manner...It almost seems more like a fungal infection....maybe it's

Fungal-bacterial endosymbiosis ...

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2729545/

https://en.wikipedia.org/wiki/Mucormycosis

That's interesting. Do the Red Cross object to anybody who was in the UK during the 80s? Where there were more cases than anywhere else if I remember right. (nice to think we still lead the world in some things ).

I've lived in UK all my life and give blood regularly. They've never refused it on those grounds.

Vampires can't be too choosy.

Red Cross in Australia has complete moratorium on donors who were in Europe during the years of the Mad Cow disease outbreak.

I know of many that were there for only a short time and now are excluded from donation.

Wow: I had no idea. This makes it very difficult when you live in Europe; finding donors who were't here for the duration.

I wonder if we have some kind of testing.

The question remains: What do you test for? Mycobacteria? Fungal spores? Prions?

Viruses?

This issue with scrapie being helped with zinc supplement, almost reminds one of leaky bowel syndrome in humans.

It pays to pay attention to the state of one's health, often there exists a precipice beyond that slippery slope of not taking care of one's health.

I think the European red cross must have just accepted the general risk and takes donors. The Aus Red Cross Blood bank (ARCBB) does have fairly thorough screening, but also has the challenge to meet demand. They even exclude some areas of Aus in particular seasons for Malaria and other mosquito transmitted diseases.

You may gather that I'm a donor. Looks like I'll hit 250 total donations during next year, though I now donate plasma instead of whole blood.

Interesting thread. This is truly complex set of diseases, and immunity protocols do not seem to exist.

If it really is bacterial, then it could spread perhaps further than previously supposed.

Well, I find your article interesting.

I have always thought it odd that scrapie in sheep can be caused by zinc deficiency (well treated by zinc supplementation), perhaps the cause is something more obscure (such as gut imbalance).

And then it is passed on to cows. I could not understand that mechanism.

Well zinc is commonly used in viral mitigation....and a myriad of other maladies...

..."Zinc is used for treatment and prevention of zinc deficiency and its consequences, including stunted growth and acute diarrhea in children, and slow wound healing. It is also used for boosting the immune system, treating the common cold and recurrent ear infections, and preventing lower respiratory infections."...

https://www.webmd.com/vitamins-supplements/ingredientmono-982-zinc.aspx?activeingredientid=982

https://well.blogs.nytimes.com/2011/02/15/for-cold-virus-zinc-may-edge-out-even-chicken-soup/

Interesting article. Thanks for posting this. I thought it was caused by a virus. I had not heard of a transmissible protein before. It's a scary situation whether it's a prion, a bacterium, or a virus. I have a friend with Parkinson's, and a sister has a friend with dementia. Nutrition can delay, but probably not cure either. Old age is sneaking up.

Yes to me it seems the better state of health you're in, generally speaking, the longer it takes these diseases to develop...but then the older you get the harder it is to keep your health optimum as the system starts to fail...certainly diet and exercise play key roles here....

prion diseases...and associated

..."While PrP is considered the only mammalian prion, prion-like domains have been found in a variety of other mammalian proteins. Some of these proteins have been implicated in the ontogeny of age-related neurodegenerative disorders such as amyotrophic lateral sclerosis (ALS, known as Motor Neurone Disease outside the US), frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U), Alzheimer's disease, and Huntington's disease,^[76] as well as some forms of Systemic Amyloidosis including AA (Secondary) Amyloidosis that develops in humans and animals with inflammatory and infectious diseases such as Tuberculosis, Crohn's disease, Rheumatoid arthritis, and HIV AIDS. AA amyloidosis, like prion disease, may be transmissible.^[77] This has given rise to the 'prion paradigm', where otherwise harmless proteins can be converted to a pathogenic form by a small number of misfolded, nucleating proteins.^[78]

^{The definition of a prion-like domain arises from the study of fungal prions. In yeast, prionogenic proteins have a portable prion domain that is both necessary and sufficient for self-templating and protein aggregation. This has been shown by attaching the prion domain to a reporter protein, which then aggregates like a known prion. Similarly, removing the prion domain from a fungal prion protein inhibits prionogenesis. This modular view of prion behaviour has led to the hypothesis that similar prion domains are present in animal proteins, in addition to PrP.[76] These fungal prion domains have several characteristic sequence features. They are typically enriched in asparagine, glutamine, tyrosine and glycine residues, with an asparagine bias being particularly conducive to the aggregative property of prions. Historically, prionogenesis has been seen as independent of sequence and only dependent on relative residue content. However, this has been shown to be false, with the spacing of prolines and charged residues having been shown to be critical in amyloid formation.[5]}

^{Bioinformatic screens have predicted that over 250 human proteins contain prion-like domains (PrLD). These domains are hypothesized to have the same transmissible, amyloidogenic properties of PrP and known fungal proteins. As in yeast, proteins involved in gene expression and RNA binding seem to be particularly enriched in PrLD's, compared to other classes of protein. In particular, 29 of the known 210 proteins with an RNA recognition motif also have a putative prion domain. Meanwhile, several of these RNA-binding proteins have been independently identified as pathogenic in cases of ALS, FTLD-U, Alzheimer's disease, and Huntington's disease.[79]"....}

https://en.wikipedia.org/wiki/Prion

I find that my eyesight is getting worse and worse with old age.

Easily remedied by pressing Ctrl and the + key on the keyboard....

That's good to know. I'll try to avoid eating any cannibals.

The hypothesis cited in the OP that TSE's may be caused by bacteria was made in 2004 but has not been validated. So although we may be uncomfortable with the wierdness of prion disease, the current consensus is still that prions are the cause.

There's a very straightforward outline of the biology of prions/disease (dated 2017) to be found here:

http://www.biology-pages.info/P/Prions.html

Interesting that there is a genetic susceptibility factor, evidently involving just one amino acid substitution.

As regards the importance of zinc, this is not surprising since metal ions are involved in many chaperone molecules for protein folding, and 'zinc fingers' identified in nature are also the subject of engineering for the purpose of gene editing therapy. Not sure how firm the statistical knowledge is, but I have read that 1% of human genes contain zinc fingers; and that 25% of protein folding requires a metallochaperone molecule (copper and manganese are also involved).

If you google zinc fingers you'll find lots of relevant information.

Here's a link with multiple articles:

https://www.sciencedirect.com/topics/neuroscience/zinc-finger

Yes the folded prions are transmissible, but what causes the folding initially is the question...this may be the information that leads to effective treatment, of which there are none....

..."In the human form of mad cow disease, called Creutzfeldt-Jakob, a person's brain deteriorates—literally developing holes that cause rapidly progressing dementia. The condition is fatal within one year in 90 percent of cases. The culprits behind the disease are prions—misfolded proteins that can induce normal proteins around them to also misfold and accumulate. Scientists have known that these self-propagating, pathological proteins cause some rare brain disorders, such as kuru in Papua New Guinea. But growing evidence suggests that prions are at play in many, if not all, neurodegenerative disorders, including Alzheimer's, Huntington's and Parkinson's, also marked by aggregations of malformed proteins.

Until recently, there was no evidence that the abnormal proteins found in people who suffer from these well-known diseases could be transmitted directly from person to person. The tenor of that discussion suddenly changed this September when newly published research in the journal Nature provided the first hint such human-to-human transmission may be possible.

For the study, John Collinge, a neurologist at University College London, and his colleagues conducted autopsies on eight patients who died between the ages of 36 and 51 from Creutzfeldt-Jakob. All the subjects had acquired the disease after treatment with growth hormone later found to be contaminated with prions. The surprise came when the researchers discovered that six of the brains also bore telltale signs of Alzheimer's—in the form of clumps of beta-amyloid proteins, diagnostic for the disease—even though the patients should have been too young to exhibit such symptoms.

These observations suggest that the tainted hormone injections might have carried small amounts of beta-amyloid proteins that triggered the formation of more such proteins. Neither Alzheimer's nor any known human prion diseases are contagious through direct contact. Yet human transmission of prion diseases has occurred through certain medical procedures and, in the case of kuru, cannibalism. The new study therefore raises the possibility that Alzheimer's is a transmissible disease with an etiology akin to prion diseases."...

https://www.scientificamerican.com/article/are-prions-behind-all-neurodegenerative-diseases1/

http://www.iflscience.com/health-and-medicine/new-prion-disease-raises-questions-about-whether-alzheimer-s-and-parkinson-s/

So it seems that all of these neurodegenerative diseases may be caused by abnormal prions and be person to person transmissible....this is indeed a very frightening thought...

"Person to person" transmission is only possible with an exchange of neural tissue. Definitely scary if you're thinking of having brain surgery any time soon. Maybe any surgery? I'm not sure. Surgical instruments which are not purged of the misfolded material are the likely means of transmitting the disease.

https://www.nature.com/news/the-red-hot-debate-about-transmissible-alzheimer-s-1.19554

"Amyloids stick like glue to metal surgical instruments, and normal sterilization does not remove them, so amyloid seeds might possibly be transferred during surgery.....
"If further research does confirm that common neurodegenerative diseases are transmissible, what then? One immediate priority would be rigorous sterilization procedures for medical and surgical instruments that would destroy amyloids, in the way that extremely high temperatures and harsh chemicals destroy prions. Aguzzi says that funding agencies should put out calls now to researchers to develop cheap and simple sterilization methods. “It's not very sexy science, but it is urgently needed,” he says. "

I think the recent work is showing that transmission is more likely possible, that can only mean that they better get it off the scalpels and such!

Well it's odd that some prion diseases are shown to be transmissible through bodily excretion, blood and other materials, and some are thought not to spread as easily....it's not that the prions don't exist in these materials, because they do, it seems to be more about the dose acquired....one has to wonder if this is accumulative in nature...

..."Prion diseases range from being highly infectious, for example scrapie and CWD, which show facile transmission between susceptible individuals, to showing negligible horizontal transmission, such as BSE and CJD, which are spread via food or iatrogenically, respectively. Scrapie and CWD display considerable in vivo dissemination, with PrPSc and infectivity being found in a range of peripheral tissues. This in vivo dissemination appears to facilitate the recently reported excretion of prion through multiple routes such as from skin, feces, urine, milk, nasal secretions, saliva and placenta. Furthermore, excreted scrapie and CWD agent is detected within environmental samples such as water and on the surfaces of inanimate objects. The cycle of “uptake of prion from the environment—widespread in vivo prion dissemination—prion excretion—prion persistence in the environment” is likely to explain the facile transmission and maintenance of these diseases within wild and farmed populations over many years."..

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3268960/

..."CJD is classified as a transmissible spongiform encephalopathy (TSE) in humans; other TSEs in humans include kuru, Gerstmann-Straussler-Scheinker syndrome, and fatal familial insomnia syndrome (table 1). In recent years, a new variant form of CJD (vCJD) has been recognized. vCJD differs from CJD in many respects, including epidemiology, pathology, and geographic distribution (primarily in the United Kingdom). In addition to these 4 prion diseases in humans, 6 prion diseases in animals have been described: scrapie in sheep and goats, transmissible mink encephalopathy, exotic ungulate encephalopathy, chronic wasting disease of mule deer and elk, feline spongiform encephalopathy, and bovine spongiform encephalopathy (BSE, also known as “mad cow disease”). "...

..."CJD and other transmissible spongiform encephalopathies exhibit an unusual resistance to conventional chemical and physical decontamination methods [3]. Because CJD is not readily inactivated by conventional disinfection and sterilization procedures, and because of the invariably fatal outcome of CJD, the procedures for disinfection and sterilization of the CJD prion have been both conservative and controversial for many years. The purpose of this article is to critique the literature and develop evidence-based guidelines to prevent cross-transmission of infection from CJD-contaminated medical devices."...

Prions are nearly impossible to destroy...

Creutzfeldt-Jakob Disease: Recommendations for Disinfection and Sterilization

https://academic.oup.com/cid/article/32/9/1348/291736

I think this is an informative post and it is very useful and knowledgeable. therefore, I would like to thank you for the efforts you have made in writing this article.

Just a slight correction to the title, by a bacterium or by bacteria.

I'm sure I don't know what you are referring to...