A prion is an infectious agent consisting of a protein that is mis-folded. It can cause several central nervous system diseases. Included are Creutzfeldt-Jakob Disease, Fatal Familial Insomnia and Kuru in humans plus Scrapie in sheep.

539 Questions

How do prions reproduce?

They don't quite 'reproduce', propagate would be closer to the mark. Prions are 'rogue' proteins, versions of naturally occurring proteins with a different 3D structure.

They replicate in living host .


What organic molecule is a prion?

A prion is a misfolded protein that fosters misfolding in other normal proteins, thereby resulting in disease.


How are prions different from other microorganisms?

They contain only protein and no nucleic acids


Are prions a virus a bacteria or a protist?

A virus is a self-assembling collection of proteins and genetic material, a bacteria is a free-living single cell and a protist is a complex organism consisting of multiple cells. Prions are mis-folded proteins, so they would be classified as none of the above. Their discovery in the 1970s by a researcher in California was dismissed until the discovery of BSE in cattle in the late 1980s in the United Kingdom, because they were a novel method of infection.


Differentiate between prions and viroids?

Simply put a prion is a pathogen that consists only of protein and only infect animals. while viroids are made only of RNA and only infect plants.


How does a prion differ from a virus?

Prions are different because they do not infect and replicate in the same way that viruses do. Viruses have RNA or DNA components and use body cells to replicate in. Prions are infectious proteins and they cause a structural change to other proteins that they interact with and that is how they cause damage. Probably the most famous prion disease is Bovine Spongiform Encephalitis (mad cow) where the structural change that the prion causes to the proteins in the brain causes holes to appear in the tissue, making it look like a sponge.


How can you prevent prion diseases?

in order to answer this question, you must first determine where the PRION is coming from. What causes the (any infected body) protein to begin the mal folding process? Or is the prion simply ingested from diseased tissue? (beef, sheep, goat..... and which tissue? And why were cannibals suseptible? What cannibal source initiated the disease? (brain tissue, or affected motor related, ie nerve related matter?) If incubation is two to twenty three years....?? what implications does that factor suggest?

where or what is the source of the deadly protein...that is the question.


Is a prion living?

This could be a real gray area depending on the definition of life.

I would have to say yes as they meet the following criteria.

  • they reproduce.
  • they employ enzymes (themselves)
  • they utilized energy to perpetuate their function
  • they utilized resources to perpetuate their function.

What is a prion vector?

Eating the meat - and especially the brains and other nervous tissue - of diseased animals.


Do prions reproduce?

Not in the sense that organisms reproduce, no. However, they can propagate and multiply. A prion can rearrange the structure of a normal protein, causing it to become a prion as well (which is why it is an infectious agent).


Do prions contain DNA or RNA?

Prions are an infectious particle made of protein. They do not contain DNA or RNA.


How do prions infect the body and cause disease?

Prions are protein matrices that self replicate. they are not alive and are not easily denatured using heat. Example = "mad cow disease"

These matrices can become quite large and cause inflammation and then necrotic areas in the body.


Can prions be destroyed by cooking?

No, cooking does not destroy or disable prions. If you were able to cook a meat that contains prions to the point where the prions were disabled, the meat would be rendered inedible.

You can use chemicals mixed with heat to destroy prions, but that's not a process you would want to subject your food to.


Is smallpox a bacteria virus or prion?

A virus; the Variola Virus. mirin' my knowledge ? ye, u mirin'


What do viruses and prions have in common?

Both are non cellular .


How do prions differ from viruses?

Viruses are non cellular infectious entities which possess DNA or RNA as heredity material enclosed in a protein capsid. Different viruses attack plants animals and bacteria and cause diseases.Viruses are intermediate between living and non living things.

Prions are protein molecules discovered in 1983 that cause mad cow disease and brain infection.They are self replicating by unknown mechanism.


How are viroids and prions the same?

Both Viroids and Prions have nucleic acid, but Viroids have no outer protein coat.


Are prions eukaryotic?

Prions are not eukaryotic. In fact, prions aren't even alive. They are merely an infectious protein, like a virus or a viroid. A commonly known prion is the mad cow disease.


What is a prion?

PrionsA prion is an infectious protein that is misfolded. These proteins can aggregate in the brain and other neural tissue, forming amyloids. Diseases associated with prions include bovine spongiform encephalopathy (mad cow disease), scrapie, kuru, chronic wasting disease, and Creutzfeldt-Jakob disease. Prions are still poorly understood by researchers, and prion diseases (transmissible spongiform encephalopathies) remain untreatable.

Is DNA found in all prions?

No, DNA is not found in any prions. Prions are just protein - they don't contain a nucleic acid.


What is the treatment for prion disease?

There is no known effective treatment to arrest or cure prion diseases. Treatment focuses on alleviating the patient's symptoms, increasing their comfort, and palliative care.


How do people get sporadic prion disease?

Patients with sporadic prion diseases may have a susceptibility polymorphism in their PRNP gene, and may have spontaneous mutations forming prion proteins.


What is the difference between virions and prions?

Prions are infectious agents composed exclusively of a single sialoglycoprotein called PrP 27-30. They contain no nucleic acid. PrP 27-30 has a mass of 27,000 - 30,000 daltons and is composed of 145 amino acids with glycosylation at or near amino acids 181 and 197. The carboxy terminus contains a phosphatidylinositol glycolipid whose components are ethanolamine, phosphate, myo-inositol and stearic acid. This protein polymerizes into rods possessing the ultrastructural and histochemical characteristics of amyloid. Amyloid is a generic term referring to any optically homogenous, waxy, translucent glycoprotein; it is deposited intercellularly and/or intracellularly in many human diseases such as:

  • Alzheimer's disease
  • Creutzfeldt-Jakob disease
  • Down's syndrome
  • Fatal familial insomnia
  • Gerstmann-Straussler syndrome
  • Kuru Leprosy

Viroids are infectious agents composed exclusively of a single piece of circular single stranded RNA which has some double-stranded regions.

  • Because of their simplified structures both prions and viroids are sometimes called subviral particles. Viroids mainly cause plant diseases but have recently been reported to cause a human disease.

    Catalytic RNAs are those that have the intrinsic ability to break and form covalent bonds; Viroids are catalytic RNA's (ribozymes) that cleave RNA to produce fragments containing a 5'-hydroxyl and a 2', 3'-cyclic phosphate.


What are different prion diseases?

Some examples of infectious prion diseases include scrapie in sheep and goats, kuru in cannibalistic humans of Papua New Guinea, and BSE, or mad cow disease, which is transmitted to humans through infected beef products.

Alzheimer's Disease is a transmissible prion/protein disease.

Researchers injected mice with brain matter from an AD victim and the mouse developed brain lesions.(Jucker, Walker, 2010)

David Colby & Stanley Prusiner - Released January 2011 ENLARGING SPECTRUM OF PRION-LIKE DISEASES

"The discovery that prions form amyloid prompted one of us to suggest that the common neurodegenerative diseases are also caused by prions (Prusiner 1984; Prusiner 2001) despite the inability to transmit such illnesses to monkeys and apes (Goudsmit et al. 1980).

"Taken together, these findings argue that prion-like, self-propagating states feature in many different, if not all, neurodegenerative diseases."

Regarding transmission to monkeys and apes, in 2007 in the UK, researchers injected marmosets with AD brain homogenates, and some of the animals developed AD-like amyloid plaques (Baker, Ridley, et al 2007)

Alzheimer's is a prion disease:

Recently Nobel Laureate Stanley Prusiner and Dr. Warren Olanow said Parkinson's Disease (PD - 1 million victims) is also most likely a prion disease:

"It is thus possible that PD is a prion disorder resulting from increased production and/or impaired clearance of

proteins such as a-synuclein, leading to misfolding and the formation of toxicoligomers, aggregates, and cell death.

Further, it is possible that a-synuclein is a prion protein that can self-aggregate and be transmitted to unaffected cells, thus extending the disease process.'


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