PRIONS QUIZLET

Has anyone ever survived the prion disease?

A Belfast man who suffered variant CJD - the human form of mad cow disease - has died, 10 years after he first became ill. Jonathan Simms confounded doctors by becoming one of the world's longest survivors of the brain disease.

What does prion stand for exactly?

A prion (short for proteinaceous infectious particle) is a unique type of infectious agent, as it is made only of protein.

Can you get the prion disease from chickens?

Abnormal structural changes of the prion protein (PrP) are the cause of prion disease in a wide range of mammals. However, spontaneous infected cases have not been reported in chicken.

Is Alzheimer's a prion disease?

Alzheimer's disease is a 'double-prion disorder': Self-propagating amyloid and tau prions found in post-mortem brain samples, with highest levels in patients who died young.

Which drawing depicts a normal or PrP-Sen protein?

An explanation since picture's do not work for me. In the transmissible spongiform encephalopathies, disease is closely associated with the conversion of the normal proteinase K-sensitive host prion protein (PrP-sen) to the abnormal proteinase K-resistant form (PrP-res). Amino acid sequence homology between PrP-res and PrP-sen is important in the formation of new PrP-res and thus in the efficient transmission of infectivity across species barriers. It was previously shown that the generation of mouse PrP-res was strongly influenced by homology between PrP-sen and PrP-res at amino acid residue 138, a residue located in a region of loop structure common to PrP molecules from many different species. In order to determine if homology at residue 138 also affected the formation of PrP-res in a different animal species, we assayed the ability of hamster PrP-res to convert a panel of recombinant PrP-sen molecules to protease-resistant PrP in a cell-free conversion system. Homology at amino acid residue 138 was not critical for the formation of protease-resistant hamster PrP. Rather, homology between PrP-sen and hamster PrP-res at amino acid residue 155 determined the efficiency of formation of a protease-resistant product induced by hamster PrP-res. Structurally, residue 155 resides in a turn at the end of the first alpha helix in hamster PrP-sen; this feature is not present in mouse PrP-sen. Thus, our data suggest that PrP-res molecules isolated from scrapie-infected brains of different animal species have different PrP-sen structural requirements for the efficient formation of protease-resistant PrP.

Which drawing depicts a disease causing or PrP-res protein?

An explanation since pictures does not work for me. Transmissible spongiform encephalopathies (TSEs or prion diseases) are a rare group of invariably fatal neurodegenerative disorders that affect humans and other mammals. TSEs are protein misfolding diseases that involve the accumulation of an abnormally aggregated form of the normal host prion protein. They are unique among protein misfolding disorders in that they are transmissible and have different strains of infectious agent that are associated with unique phenotypes in vivo. A wealth of biological and biophysical evidence now suggests that the molecular basis for prion diseases may be encoded by protein conformation.

What is BSE?

BSE is a disease which affects the nervous system of cattle and kills them. BSE is an abbreviation for 'bovine spongiform encephalopathy'.

How is prion disease different from a bacterial infection?

Bacteria are microorganisms that contain genetic material. They do not generate spontaneously. In contrast, Prion Disease is caused by a change in shape of a cellular protein. The resulting pathogenic prion proteins begin to recruit and change normal proteins into an abnormal shape.

What is Chronic Wasting Disorder?

Chronic wasting disease (CWD) is a prion disease that affects deer, elk, reindeer, sika deer and moose. It has been found in some areas of North America, including Canada and the United States, Norway and South Korea.

What is CJD?

Creutzfeldt-Jakob disease (CJD) is a rare, degenerative, fatal brain disorder.

What is Fatal Familial Insomnia?

Fatal familial insomnia (FFI) is a rare genetic degenerative brain disorder. It is characterized by an inability to sleep (insomnia) that may be initially mild, but progressively worsens, leading to significant physical and mental deterioration.

Can you cook prions out of British Beef?

In addition, normal disinfection procedures do not stop this disease, so even well-cooked contaminated meat can infect humans. The rendering process - cooking of dead, often disease-ridden, animals - used to make supplements for animal feed, also cannot kill the infection, and only serves to spread it.

What is Kuru?

Kuru is a very rare disease. It is caused by an infectious protein (prion) found in contaminated human brain tissue. Kuru is found among people from New Guinea who practiced a form of cannibalism in which they ate the brains of dead people as part of a funeral ritual.

How long can you live or survive having prion disease?

Most people with CJD die within 6 to 12 months after symptoms appear. About 10 to 20% of people survive for 2 years or more. People with vCJD usually survive for about 18 months.

What is prion disease?

Prion diseases or transmissible spongiform encephalopathies (TSEs) are a family of rare progressive neurodegenerative disorders that affect both humans and animals.

Are there good prions?

Researchers have found nearly 50 helpful prions in yeast and comparable proteins in humans, suggesting that this dreaded protein type can boost survival and plays a role in evolution.

What is the earliest documentation of prions?

Scrapie, a disease affecting sheep and goats, was the first prion disease to be identified in 1732.

Can the immune system fight prions?

Strong evidence demonstrates a significant role of innate immunity in both combatting and abetting peripheral prion pathogenesis.

What are the symptoms of prion disease?

Symptoms of prion diseases include: Rapidly developing dementia. Difficulty walking and changes in gait. Hallucinations. Muscle stiffness. Confusion. Fatigue. Difficulty speaking.

What is the formal name for all prion diseases in humans?

The human forms of prion disease are most often the names Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gertsmann-Straussler-Scheinker syndrome (GSS), kuru and variably protease-sensitive prionopathy (VPSPr).

Where are normal prion proteins found?

The normal form of the prion protein PrP is found on the surface of nerve cells, but when it changes into its misfolded form, it aggregates into long fibrils that clog up the normal functioning of the brain.

how many different prion diseases are there?

The process of prion propagation in the brain results in the pathogenesis of prion diseases [6]. Sixteen different variants of prion disease have been reported so far: nine in humans and seven in animals.

Do we all have prions?

The protein that prions are made of (PrP) is found throughout the body, even in healthy people and animals. However, PrP found in infectious material has a different structure and is resistant to proteases, the enzymes in the body that can normally break down proteins.

How can you kill a prion?

To destroy a prion it must be denatured to the point that it can no longer cause normal proteins to misfold. Sustained heat for several hours at extremely high temperatures (900°F and above) will reliably destroy a prion.

How is prion disease different from a viral infection?

Viruses are microorganisms that contain genetic material. They do not generate spontaneously. In contrast, Prion Disease is caused by a change in shape of a cellular protein. The resulting pathogenic prion proteins begin to recruit and change normal proteins into an abnormal shape.

Should I be concerned about prion disease?

Yes and no, because this abnormal accumulation of protein in the brain can cause memory impairment, personality changes, and difficulties with movement. Experts still don't know a lot about prion diseases, but unfortunately, these disorders are generally fatal.

What is scrapie?

a disease of sheep involving the central nervous system, characterized by a lack of coordination causing affected animals to rub against trees and other objects for support, and thought to be caused by a virus-like agent such as a prion.

What is a prion?

a type of protein that can trigger normal proteins in the brain to fold abnormally.

What is a spongiform disease?

any of various degenerative diseases of the brain characterized by the development of porous spongelike lesions in brain tissue and by deterioration in neurological functioning.

What happens to the brain tissue?

the resultant deterioration of neurons causes a spongelike pattern to develop in the brain tissue. It becomes abnormal and clump in the brain, causing brain damage.