The earth is not flat, the sun does not rotate around the earth, and prions cannot be infectious if they cannot satisfy Koch’s postulates! Continuing to defend the theory that BSE and CJD are caused by and transmitted by prions is akin to defending the theory that “life and disease are the result of spontaneous generation”!
—Dr. Joel D. Wallach
Lecture Series, AD 2000
Viruses are small, simple nucleic acid molecules. They are giants compared to “viroids” which are small molecules of naked circular RNA that typically infect plants. Viroids are only several nucleotides long. Viroids do not encode proteins but can replicate in host plant cells by using the hosts cellular enzymes. The RNA molecule of the viroid disrupts the metabolism of the plant host and stunts the verticle growth of the plant. One viroid disease in coconut palms from the Philippines has killed more than ten thousand trees.
There is a theory that supports the existence of an infectious protein that are called “prions.” Prions are theorized to cause a variety of degenerative brain and spinal cord diseases in vertebrate animals including “scrapie” in sheep, mad cow disease in cattle, and Creutzfeldt-Jakob disease in humans.
One theory poses that a prion is a mis-folded form of a protein normally found in brain cells. Stanley Prusiner was awarded the 1997 Nobel Prize for his prion research. However, there is not general acceptance that a prion is an infectious protein that can produce disease by itself because this theory remains controversial.
In the late 19th century enzootic ataxia was a common disease in Australian lambs and adult sheep. The disease was first scientifically described and published in the Australian veterinary journals in 1932. The disease is characterized by poor coordination, weakness, and demyelinating lesions in the spinal cord. This has been reported in Western Australia, South Australia, and Victoria.
In addition to neurological symptoms and lesions found in enzootic ataxia, there is also a loss of wool quality known as “straight steely” wool. Further investigation showed that sheep producing steely wool were in fact showing clinical effects of a copper deficiency. It was also demonstrated that breeding ewes with steely wool resulted in lambs being born with enzootic ataxia. In fact, maps have been created that have documented effects of copper deficiency, such as ataxia in lambs, steely wool in adult sheep, and copper deficiency in plants.
Copper deficiency enzootic ataxia can present in lambs from the time of birth to about four months of age. In England most of the lambs have been afflicted at birth, but some do not show ataxia symptoms until two weeks up to six weeks of age.
Bovine spongiform encephalitis, popularly known as BSE (Bovine Spongioform Encephalitis) or “Mad Cow Disease,” is believed to be transmitted from one animal to the next and to humans by an infectious “agent” referred to as a prion. In humans, the disease was originally known as Kuru (thought to be passed on from one human to the next by the practice of mortuary cannibalism) or Creutzfeldt-Jacob Disease when acquired by eating “contaminated beef.”
The normal cellular form of prion protein (PrPc) is generally thought to be a precursor to the pathogenic protease-resistant forms (PrPsc) believed to cause scrapie (thought to be a long incubation viral encephalopathy of sheep), bovine spongiform encephalopathy (BSE), and Creuttzfeldt-Jacob disease in humans. Its amino acid terminus contains the octapeptide PHGGGWGQ, which is repeated four times and is among the best-preserved regions of mammalian PrPc.
The amino-terminal domain of PrPc exhibits five to six sites that bind copper (Cu(II)) presented as a glycine chelate. At neutral pH, binding occurs with positive cooperativity, with binding affinity compatible with estimates for extracellular, labile copper. Two lines of independently derived PrPc gene-ablated (Prnp o/o) mice exhibit severe reductions in the copper content of membrane-enriched brain extracts and similar reductions in synaptosomal and endosome-enriched subcellular fractions.
Despite the mass of accumulated biochemical and structural information describing prions, Koch’s Postulates have not been fulfilled because transmission attempts from positively diagnosed cattle and humans to susceptible species have universally failed. BSE and CJD are therefore copper deficiency diseases and are not infectious diseases!
Most reported cases of BSE in cattle are reported in the United Kingdom in the southern one third of the island and predominantly in dairy cattle. Now, how does an infectious organism determine which cow is a dairy cow and which cow is a beef cow? Attempts to satisfy Koch’s postulates for BSE and CJD have been abysmal failures—literally thousands of attempts were performed by juicing the brains of “infected” cattle and injecting them into the brains of healthy cattle with no positive signs of transmission. Extracts of Creutzfeldt-Jacob Disease brains from “infected” humans have been injected into primates, including chimpanzees and monkeys, and these attempts have failed to transmit the disease. Thus they have failed to satisfy Koch’s postulates.
It is obvious that the brain lesions in sheep afflicted with enzootic ataxia, a known copper-deficiency disease, are identical to the brain lesions in cattle afflicted with BSE and also to the brain lesions in humans afflicted with CJD. The preponderance of the cases of BSE in cattle and CJD in humans are typically diagnosed in geographical areas where the soils are copper deficient.
It is also common for humans with CJD to be afflicted with concurrent copper deficiency signs, symptoms, and diseases, for example with white, gray, or silver hair and vitaligo, wrinkles, connective tissue disease, anemia, hypothyroidism, spider veins, varicose veins, hemorrhoids, and aneurysms.
Continuing to defend the theory that BSE and CJD are caused by and transmitted by prions is akin to defending the theory that scurvy and pellagra were caused by germs, and that life and disease are caused by spontaneous generation!