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Hidden Prions a Public Health Threat Say Experts
By showing that spleen tissue is up to sevenfold more receptive to foreign prions than that of the brain, Vincent Béringue PhD, and colleagues at the Institut National de la Recherche Agronomique (INRA) in Jouy-en-Josas, France, recently challenged the long-held notion of absolute species barriers. What this suggests is that testing brain tissue, rather than lymphatic tissue, of animals destined for the dinner table is very misleading. Furthermore, say these scientists, most prion disease will likely remain silent for the lifetimes of the hosts, making infection very difficult to spot.
* Species-Jumping Prions Propagate Silently in Lymphoid Tissue With no Detectable Signs of Brain Disease....
* Experts Call for Expanded Prion Surveillance....
* Silent Infection with vCJD....
* Prions Spread Within Species and Across Species Barriers....
* Why a More Aggressive Search for Prions is So Important
It now appears that not only is the transmission barrier keeping these odd pathogenic proteins from easily jumping to you from that steak on your plate more porous than previously thought, it also seems that authorities might not always be testing the right tissue. As William A. Rutala PhD and David J. Weber MD point out in their 2010 paper: “Prion diseases elicit no immune response, result in a pathologic process confined to the central nervous system, have an incubation period of years, and usually are fatal within 1 year after diagnosis.” These are not diseases to be treated casually.
Misfolded protein aggregates: mechanisms, structures and potential for disease transmission.
Some of the most prevalent human degenerative diseases appear as a result of the misfolding and aggregation of proteins. Compelling evidence suggest that misfolded protein aggregates play an important role in cell dysfunction and tissue damage, leading to the disease. Prion protein (Prion diseases), amyloid-beta (Alzheimer's disease), alpha-synuclein (Parkinson's disease), Huntingtin (Huntington's disease), serum amyloid A (AA amyloidosis) and islet amyloid polypeptide (type 2 diabetes) are some of the proteins that trigger disease when they get misfolded. The recent understanding of the crucial role of misfolded proteins as well as the structural requirements and mechanism of protein misfolding have raised the possibility that these diseases may be transmissible by self-propagation of the protein misfolding process in a similar way as the infamous prions transmit prion diseases. Future research in this field should aim to clarify this possibility and translate the knowledge of the basic disease mechanisms into development of novel strategies for early diagnosis and efficient treatment.
The Risk of Prion Zoonoses.
Prions are lethal infectious pathogens that cause neurodegenerative diseases in humans and animals (1). They can pass from one species to another but with greater difficulty than transmission within the same species because of the so-called species barrier effect. Such barriers protect humans from developing prion disease after dietary or other exposure to animal reservoirs of infection. These include endemic scrapie of sheep and goats, chronic wasting disease (CWD) of deer and elk, and bovine spongiform encephalopathy (BSE) or “mad cow disease” (1). On page 472 of this issue, Béringue et al. (2) show that in transgenic mice expressing ovine or human prion protein (PrP), lymphoid tissue is more susceptible to cross-species transmission than neural tissue (brain), which may prompt a reevaluation of the effectiveness of species barriers.
Facilitated Cross-Species Transmission of Prions in Extraneural Tissue.
Prions are infectious pathogens essentially composed of PrPSc, an abnormally folded form of the host-encoded prion protein PrPC. Constrained steric interactions between PrPSc and PrPC are thought to provide prions with species specificity and to control cross-species transmission into other host populations, including humans. We compared the ability of brain and lymphoid tissues from ovine and human PrP transgenic mice to replicate foreign, inefficiently transmitted prions. Lymphoid tissue was consistently more permissive than the brain to prions such as those causing chronic wasting disease and bovine spongiform encephalopathy. Furthermore, when the transmission barrier was overcome through strain shifting in the brain, a distinct agent propagated in the spleen, which retained the ability to infect the original host. Thus, prion cross-species transmission efficacy can exhibit a marked tissue dependence.
Never heard of this but I think it would be wise to take it into consideration.
Will it kill the Prions if you cook your food properly or should I just go ahead and become a vegetarian? The more I learn about eating dead animals and the way we prepare food the closer I am to making the jump. Can you get this from fish or vegetables?
Are prion infections limited to just what someone can pick up from eating animal flesh? I remember reading somewhere that irradiation also creates prions in food--which has me thinking--I love to put dried oregano in my salads. Spices, unless stated otherwise, are generally irradiated...
This is a deeply disturbing finding - prion diseases are frightening.
Since most animal species utilize the same protiens, it's not really suprising that prions can jump species.
I wonder when big pharma will come up with a new vaccine to infect us all when their fear mongering ways realize there is money to be made.
This information and fear mongering comes from mainstream medical, and yet so many will believe it without consideration.
Has it ever occurred to any of you that a certain prion could be an evolutionary element that certain genetic codes will adapt to, thereby altering DNA structure to something never before seen? You all have a mind and soul of your own- use them and learn to understand the infinite possibilities of the Universe.