The media promotes prions as the cause of Mad Cow Disease, CJD, BSE and TSEs, as if the etiology were an established fact. Not so. The most likely cause is spiroplasmas.

Spiroplasmas are researched by Frank O. Bastian, MD, professor of pathology who was previously director of neuropathology at the University of South Alabama, Mobile but is now at Tulane University, New Orleans. His description of spiroplasmas is this:

"Spiroplasmas are similar to mycoplasmas in that they do not have a cell wall and have among the smallest genomes of any living organisms. Spiroplasmas, which were only discovered in 1976, are present in the hemolymph of almost all insects. There probably are several million strains of spiroplasmas. They are very fastidious organisms. Many spiroplasmas grow at fairly low temperatures. A few strains grow at 37° C, human body temperature. Many spiroplasmas cause diseases in plants."(1)

As evidence of spiroplasma etiology for TSEs, Dr. Bastian says,

"spiroplasmas contain internal fibrillar proteins (Fig 4@1), that have morphological and immunological similarities to scrapie- and CJD-related fibrillar proteins. This comparison is noteworthy since mycoplasmologists consider these fibril proteins unique to this prokaryote.

In vivo and in vitro experimental Spiroplasma infections produce cytopathic effects similar to those of the scrapie agent. Experimental Spiroplasma brain infection in the suckling rat is characterized by vacuolar encephalopathy with localization of the microbe to gray matter.

...Spiralins are chemically bound to Spiroplasma-associated fibrils (SpFs) and are separated with difficulty.' SpFs are unique internal fibrils of spiroplasmas with a molecular weight of 55 kDa. Recently, SpFs have been shown to bear close morphological resemblance to scrapie-associated fibrils (SAFS), ' and show cross-reactivity using SAF antibody."(2)

And why not Prions?

"The prion is a red herring. Prions are thought to be self-replicating proteins. Some researchers believe prions are the cause of CJD and related illnesses because they have found prions in brain tissue from people with CJD and sheep with scrapie but not in normal brain tissue. A shortcoming in the prion theory is that CJD and scrapie can be transmitted without prions. Brain material from which the prion has been removed with antibodies can still infect animals. Moreover, the prion has been found in unrelated disease processes, such as Kawsaski syndrome and inclusion body myositis.

The protein that some researchers believe causes CJD and related illnesses is a reconfigured normal host protein. Studies have shown that if you take the gene for the normal protein out of the mouse, the mouse does not develop spongiform encephalopathy when injected with infectious material."(1)

My way of saying it is that a protein (the prion) cannot acquire the characateristics of an infectious agent, because no evolution can be involved in its disease causing properties. The DNA for prions belongs to the host. Hosts cannot evolve their own diseases, beyond chance point mutations. So-called prion diseases are way too complex for that. They show strain variations in addition to complex pathology. A variety of random mutations would not continually improve the pathology. When the host holds the DNA, selection works for the host and against the disease. This means that the assumed cause of the problem, which was livestock carcasses being fed back to livestock, could not have caused the disease to adapt and become the problem that it has, if prions were the disease-causing agent.

A Convincing Research Article in PDF (1.2Mb)
Study on experimental infections of Spiroplasma mirium from the Chinese mitten crab in crayfish, mice and embryonated chickens - pdf