2041 Composed of abnormal forms of host protein, prion protein.

Prion protein is normally present in neurons.

Infectious proteins with amyloid features.

The primary route of prion infection in kuru and bovine spongiform encephalopathy is through the digestive system.

Delivered via the intestines to lymph nodes and to other parts of the body, the proteins in a prion conformation stimulate other proteins to adopt the same configuration.

Diseases occur when prion protein undergoes changes that confer resistance to proteases.

Infectious nature of the process occurs as protease resistant prion protein promotes conversion of normal protease sensitive protein to the abnormal form.

Protease resistant prion protein promotes conversion of normal protease sensitive prion protein to an abnormal form that explains the infectious nature of associated diseases.

The accumulation of prion protein leads to neuronal damage and distinctive spongiform pathologic changes in the brain.

Protein organisms that are responsible for neurologic disease such as Kuru, Creutzfeldt-Jakob disease in humans and scrapie and bovine spongiform encephalopathy in animals.

Cause fatal, transmissible neurodegenerative processes.

A common coding polymorhism at codon 129 of the prion protein gene (PRNP), where methionine or valine may be encoded and is a strong susceptibility factor for human prion diseases.

Codon 129 heterozygosity is protected against iatrogenic and sporadic Creutzfeldt Jakob disease and kuru.

May be associated with transfusions.

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