It looks like you're using an Ad Blocker.
Please white-list or disable AboveTopSecret.com in your ad-blocking tool.
Some features of ATS will be disabled while you continue to use an ad-blocker.
Prions — the infectious, deformed proteins that cause chronic wasting disease, or CWD, in deer — can be taken up by plants such as alfalfa, corn and tomatoes, according to new research from the National Wildlife Health Center in Madison.
The research further demonstrated that stems and leaves from tainted plants were infectious when injected into laboratory mice.
…“Imagine people, wildlife or livestock eating a cereal or vegetable that could years or decades later cause an incurable, fatal brain disease.
“…There is no other deadly disease agent as bizarre or invisible.”
"Prion shape affects nature of infection"
“UCSF scientists have demonstrated for the first time that a change in the folded shape of a prion protein changes its infectious properties – including the prion’s ability to jump 'species barriers.' The research, based on studies of prion infectivity in yeast, solves one of the great puzzles about prions: If they are infectious proteins with no genetic material of their own and no ability to mutate genetically, how can a single prion exist in different strains that can cause different diseases?
…Studies of the melting temperatures of the prions and their resistance to breakdown by enzymes indicated that the conditions generated prions with different physical properties.
...shape change accounts for strain differences, and it lays the groundwork for research to determine the physical differences that allow a prion to change shape and cause different diseases. ...The studies show that a single infectious protein can adopt different, distinct, self-propagating shapes and that these conformational differences underlie the differences in prion strains.
The same protein can misfold in various ways to create new prion strains.
......Scientists have grappled for years with one of the central tenets of the protein-only hypothesis, namely, that a single prion protein, when unaltered by genetic mutation, can give rise to different strains of prions with varying infectivity and other properties. The two research groups established that the strains could be accounted for by different misfolded conformations of the same protein. ...In test tube experiments, the researchers demonstrated that the protein conformations produced at different temperatures propagated themselves as distinct strains - providing templates for the folding of other proteins into the same shapes. Further structural analyses of two of the strains confirmed that the proteins were, indeed, folded differently. ...what we are learning about how to make proteins misfold into different conformations will be directly relevant to understanding mammalian prions, and perhaps even to trying to understand the strain phenomenon in mammalian prions. This includes how strains can affect the virulence of a disease or how likely it is to jump a species.
Prion folding produces strains
PrPc (prion) expression influences the establishment of herpes simplex virus type 1 latency.
…lack of PrPc expression favors the establishment of HSV latency whereas HSV replication proceeds more efficiently in neuronal tissue that expresses this protein. The data further suggest that PrPc may be involved in a metabolic pathway that culminates in apoptosis of neurons that have been infected by neurotropic viruses.
...science needs to find ways to cure prionic diseases as prevention appears to not be effective even in the strictest of diets, now
...viral infections (or possibly inclusive of prionic, now that we are talking about it) could create significant genetic changes in people between the time they are born and the time they die. "Significant" really means that active genetic expression can be altered in this context.
The world’s ecosystems have been plunged into chaos, with some conservation biologists thinking that no system, not even the vast oceans, remains untouched by human presence. Conservation measures, sustainable development, and, ultimately, stabilization of human population numbers and consumption patterns seem to offer some hope that the Sixth Extinction will not develop to the extent of the third global extinction, some 245 mya, when 90% of the world’s species were lost.
Though it is true that life, so incredibly resilient, has always recovered (though after long lags) after major extinction spasms, it is only after whatever has caused the extinction event has dissipated. That cause, in the case of the Sixth Extinction, is ourselves — Homo sapiens. This means we can continue on the path to our own extinction, or, preferably, we modify our behavior toward the global ecosystem of which we are still very much a part. The latter must happen before the Sixth Extinction can be declared over, and life can once again rebound.
Just what do YOU propose we actually can really, and practically DO about a substance (prion) that ...could be one of the causative functions of mutation(evolution)???
Now you say they are virtually in everything organic, MAYBE THEY ARE THE REAL FORCE BEHIND THE VARIETYOF LIFE ON EARTH,
lOOK OVER YOUR OWN SHOULDER AT THE RIVER OF LIFE WHICH NEGAT YOU.
THINK WE CAN ACTUALLY EFFECT IT?