The gastrointestinal tract plays a central role in the transmissible spongiform encephalopathies. These are human and animal diseases that include bovine spongiform encephalopathy, scrapie and Creutzfeldt-Jakob disease. They are uniformly fatal neurological diseases, which are characterized by ataxia and vacuolation in the central nervous system. See mad cow disease.

Prion disease - Prion Infection
Prion diseases or transmissible spongiform encephalopathies (TSEs) are rare neurodegenerative disorders that can be acquired either by direct transmission, inherited through dominant mutations in the prion protein gene or via an unknown sporadic cause. This latter group constitutes the vast majority of cases. Like many neurodegenerative diseases the hallmarks of oxidative damage can be readily detected throughout the brain of the affected individual. However, unlike most other neurodegenerative diseases, prion diseases are connected with a dramatic loss of antioxidant defence. As abnormal protein accumulates in the diseased brain there is both an increase of oxidative substances and a loss of the defences that keep them in check. In particular the normal cellular prion protein has been shown to be an antioxidant. Conversion of this protein to the protease resistant isoform is accompanied by a loss of this antioxidant activity.
   Findings from an animal study suggest that disease-cause prions can be spread via infected skeletal muscle from deer with chronic wasting disease a wildlife illness related to mad cow disease. Whether CWD can be passed to humans is still unclear.
   Rectal tissue from patients with variant Creutzfeldt-Jakob disease (vCJD) contains prions that can transmit the infection.

Prion protein
Cellular prion protein is a glycophosphatidylinositol anchored protein, of unknown function, found in a number of tissues throughout the body, including several blood components of which platelets constitute the largest reservoir in humans. It is widely believed that a mis-folded, protease-resistant form of prion protein is responsible for the transmissible spongiform encephalopathy group of fatal neurodegenerative diseases.

BSE prion
Bovine spongiform encephalopathy.

Creutzfeldt-Jakob disease
Variant Creutzfeld-Jakob-disease (vCJD), but not bovine spongiform encephalopathy (BSE), can be transmitted to humans. Secondary transmission of vCJD via blood transfusion and other routes is probably possible. The results, which appear in the March 27th, 2006 online issue of The Lancet Neurology, are concerning because they suggest such infections have a long preclinical phase.

Prion Infection Treatment
A novel formulation of copper and hydrogen peroxide can inactivate infectious prions -- disease-causing proteins responsible for scrapie in sheep, mad cow disease, and the human form of the disease called Creutzfeldt-Jacob disease (CJD), according to Dr. Sylvain Lehmann of Institute de Genetique Humaine du CNRS, Montpelier, France. Using medical instruments contaminated by CJD or other prion diseases is a problem. Very harsh treatment such as use of sodium hydroxide or steam -- not at all compatible with delicate equipment -- may be required for sterilization. The researchers found that their copper-hydrogen peroxide formulation significantly reduced the level of prion protein in tissue samples obtained from prion-infected mouse and human brains. In addition, mice inoculated with scrapie-infected brain tissue survived for a mean of 266 days after injection into the brain with chemical combination, compared with 167 days for infected controls. Journal of Infectious Diseases, September 15, 2006.

questions
Q. is a prion a virus ?
     A. No, a prion is not a virus

Q. Can glandular extracts contain prions?
     A. This is a good question. I don't know if glandulars or glandular extracts could potentially contain prions.

Orf Virus
People who come in close contact with sheep and goats risk contracting orf virus from infected animals. Orf is a virus that leads to skin infection. Orf is not a prion.