The whispers are getting louder: Bioterrorists have weaponized Ebola. Scary, huh?
But that's just the spin. The truth is even scarier. Infectious microbes are crossing species and kingdom barriers, cross-breeding and
inter-breeding, and creating super-plagues we don't have a hope in Hades of curing, treating, or controlling.
In fact, we're entering the Plague Time, the End of Times, most accurately described as a time of accelerated evolution.
This accelerated evolutionary process started nearly a century ago with a man-made infectious prion that mimics a-smooth muscle
(a-SMA), and with a related disease named
fibromuscular dysplasia (FMD)
. Now, there are so many different prion strains and
prion-related diseases infecting every species and kingdom that evolution on this planet has become impossible to monitor.
Today, microbes - like ebola, bird flu, rabies, antibiotic resistant gonorrhea, mad cow, tobacco mosaic, you name it - are all coming together in
Infectious prions are the bridge between these microbes, and between microbes and other higher organisms like humans.
True, man creates prions - but mother nature has the ball. So now we're living in an evolutionary hurricane, accelerated to hyperspeed.
Forget bioterrorism. It's out of human hands. Living cells are better laboratories than any corporate-military super-high-tech-lab - and all the
requisite components are already loose in the world. Mother nature can "weaponize" ebola - and create other bioweapons - better and faster than any
My advice? ...Relax. And enjoy the ride. Or think of Jesus. Whatever works for you.
But drop the witchhunt. Our future is clear:
Findings suggest that neurodegenerative disease affects other tissues and raise the possibility that heart infection could be a new aspect of
prion diseases, including those that affect humans and livestock, and that these diseases could travel through the blood.
"Until now, prion disease has been thought of as a chronic neurological condition," says Scripps Research Professor Michael B. Oldstone, M.D., who
led the research. "Our study has shown, however, that it can have other manifestations, therefore expanding the types of conditions it could
According to the U.S. Centers for Disease Control and Prevention, the median age of death for Americans with Creutzfeldt-Jakob disease is 68, whereas
the median age of death of people with new variant Creutzfeldt-Jakob in Great Britain, where most cases have occurred, is 28.
Heart Damage caused by Prion Disease Agent In Mouse Study
The Sup35p protein of Saccharomyces cerevisiae is an essential translation factor whose prion-like properties give rise to the non-Mendelian genetic
element [PSI(+)]. ...These findings have important implications for ...evolution...
The Candida albicans Sup35p protein
(CaSup35p): function, prion-like behaviour and an associated polyglutamine length polymorphism.
Prions ...cause a number of infectious, genetic and spontaneous disorders. ...prions (pronounced "pree-ons") multiply in an incredible way;
they convert normal protein molecules into dangerous ones simply by inducing the benign molecules to change their shape.
...there are hints that the prions causing the diseases explored thus far may not be the only ones. Prions made of rather different proteins may
contribute to other neurodegenerative diseases that are quite prevalent in humans. They might even participate in illnesses that attack muscles.
About 10 to 15 percent of cases are inherited, and a small number are, sadly, iatrogenic...
1995: The Prion Diseases
And of course, the requisite cowboys playing with things they don't understand:
Patent: Milk protein biofilm and uses
A biofilm for preparing laminated tissue constructs comprising at least one milk protein forming a sheet like structure can be used to support at
least one layer of cells adhered to that. The biofilm allows for a easy handling of cultured cell sheets that can be used as tissue graft. The
biofilm, comprising milk proteins and at least one plasticizer, when adhered by a cell layer can form a laminated tissue construct for body tissue