Amyloid vs. Prion — What's the Difference?
Edited by Tayyaba Rehman — By Urooj Arif — Updated on May 19, 2024
Amyloid refers to abnormal protein aggregates associated with diseases like Alzheimer's, while prion is a type of infectious protein that can cause neurodegenerative disorders by inducing abnormal folding of normal proteins.
Difference Between Amyloid and Prion
Table of Contents
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Key Differences
Amyloid is a general term for insoluble protein aggregates that accumulate in tissues and organs, often leading to diseases such as Alzheimer's and Parkinson's. These deposits disrupt normal cell function and can be toxic. Prions, on the other hand, are infectious proteins that propagate by inducing misfolding in normal cellular proteins, leading to disorders like Creutzfeldt-Jakob disease.
Amyloids typically form from various proteins that misfold and aggregate, such as amyloid-beta in Alzheimer's disease. These aggregates are not inherently infectious but cause cellular damage through a variety of mechanisms. Prions are unique in that they are transmissible agents composed solely of protein, without nucleic acids, and they can spread from one individual to another, causing disease.
While amyloids can arise from multiple types of proteins and are linked to several different diseases, prions are associated specifically with a set of diseases called transmissible spongiform encephalopathies (TSEs). Prion diseases include bovine spongiform encephalopathy (mad cow disease) and kuru, in addition to human diseases like Creutzfeldt-Jakob disease.
Amyloids and prions both involve protein misfolding, but amyloids form insoluble fibrils that deposit extracellularly, whereas prions cause intracellular changes and can convert normal prion proteins into the disease-causing form. The pathological processes they induce are distinct despite some similarities in the initial misfolding events.
Comparison Chart
Definition
Insoluble protein aggregates
Infectious protein causing neurodegenerative diseases
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Disease Association
Alzheimer's, Parkinson's
Creutzfeldt-Jakob disease, mad cow disease
Mechanism
Disrupts cell function
Induces misfolding of normal proteins
Nature
Non-infectious
Infectious
Protein Formation
Various proteins
Specific prion protein (PrP)
Compare with Definitions
Amyloid
Protein deposit disrupting normal tissue function.
Amyloid buildup in the heart can cause amyloidosis.
Prion
Protein that induces misfolding in normal proteins.
Prions convert normal prion proteins into the misfolded form.
Amyloid
Substance seen in multiple systemic and localized conditions.
Amyloid can affect multiple organs, leading to systemic amyloidosis.
Prion
Agent of transmissible spongiform encephalopathies.
Prions cause mad cow disease in cattle.
Amyloid
Amyloids are aggregates of proteins characterised by a fibrillar morphology of 7–13 nm in diameter, a beta sheet (β-sheet) secondary structure (known as cross-β) and ability to be stained by particular dyes, such as Congo red. In the human body, amyloids have been linked to the development of various diseases.
Prion
Infectious protein causing neurodegenerative diseases.
Prions are responsible for Creutzfeldt-Jakob disease.
Amyloid
A starchlike substance.
Prion
Proteinaceous infectious particle without nucleic acids.
Prions spread disease through protein-protein interactions.
Amyloid
An insoluble, fibrous structure consisting chiefly of an aggregation of proteins arranged in beta sheets, forming extracellular deposits in organs or tissues and characteristic of certain diseases such as Alzheimer's disease and Parkinson's disease.
Prion
Prions are misfolded proteins with the ability to transmit their misfolded shape onto normal variants of the same protein. They characterize several fatal and transmissible neurodegenerative diseases in humans and many other animals.
Amyloid
The substance that makes up such a structure.
Prion
A protein particle that is the agent of infection in a variety of neurodegenerative diseases, including bovine spongiform encephalopathy, Creutzfeldt-Jakob disease, and scrapie. Prions are the only known infectious agents that do not contain DNA or RNA. They derive from a normal body protein that becomes irreversibly misfolded, and they proliferate in the body, possibly by acting as a template for further protein misfolding.
Amyloid
Starchlike.
Prion
(molecular biology) A self-propagating misfolded conformer of a protein that is responsible for a number of diseases that affect the brain and other neural tissue.
Amyloid
Being or related to proteinaceous amyloid
Amyloid plaque.
Prion
A petrel of the genus Pachyptila.
Amyloid
A waxy compound of protein and polysaccharides that is found deposited in tissues in amyloidosis.
Prion
Any of several types of protein particle lacking nucleic acid, believed to be the cause of certain slow-developing infectious diseases such as scapie in sheep, and Creutzfeldt-Jakob disease and Kuru in humans.
Amyloid
Any of various starchlike substances.
Prion
(microbiology) an infectious protein particle similar to a virus but lacking nucleic acid; thought to be the agent responsible for scrapie and other degenerative diseases of the nervous system
Amyloid
Containing or resembling starch.
Prion
Protein leading to brain damage and spongiform changes.
Prion diseases result in sponge-like brain tissue.
Amyloid
(mycology) Applied to a mushroom that turns blue-black upon application of Melzer's reagent
Amyloid
Resembling or containing amyl; starchlike.
Amyloid
A non-nitrogenous starchy food; a starchlike substance.
Amyloid
The substance deposited in the organs in amyloid degeneration.
Amyloid
A nonnitrogenous food substance consisting chiefly of starch; any substance resembling starch
Amyloid
(pathology) a waxy translucent complex protein resembling starch that results from degeneration of tissue
Amyloid
Resembling starch
Amyloid
Insoluble protein aggregate forming fibrils.
Amyloid plaques are characteristic of Alzheimer's disease.
Amyloid
Pathological protein clumps in various diseases.
Amyloid deposits are found in Parkinson's disease.
Amyloid
Misfolded proteins accumulating extracellularly.
Amyloid plaques interfere with neural communication.
Common Curiosities
How do prions cause disease?
Prions cause disease by converting normal prion proteins into the disease-causing misfolded form.
Are amyloids infectious?
No, amyloids are not infectious; they are protein aggregates that disrupt cell function.
What is amyloid?
Amyloid is an insoluble protein aggregate that forms in tissues, often linked to diseases like Alzheimer's.
What is a prion?
A prion is an infectious protein that causes neurodegenerative diseases by inducing misfolding in normal proteins.
How do amyloids form?
Amyloids form from various misfolded proteins that aggregate into fibrils and deposit in tissues.
Are prions infectious?
Yes, prions are infectious and can transmit disease between individuals.
What is the main protein in prion diseases?
The main protein in prion diseases is the prion protein (PrP).
Can prion diseases spread between species?
Yes, some prion diseases can spread between species, such as mad cow disease to humans.
What diseases are associated with amyloids?
Diseases such as Alzheimer's, Parkinson's, and systemic amyloidosis are associated with amyloids.
Can prion diseases be treated?
There are no effective treatments for prion diseases; management focuses on supportive care.
What diseases are associated with prions?
Prion diseases include Creutzfeldt-Jakob disease, mad cow disease, and kuru.
What is the main protein in Alzheimer's amyloid?
The main protein in Alzheimer's amyloid is amyloid-beta.
How are amyloids detected?
Amyloids are often detected through imaging techniques and biopsies.
Can amyloids be prevented?
Research is ongoing, but currently, there are no definitive ways to prevent amyloid formation.
Do amyloids affect multiple organs?
Yes, amyloids can affect multiple organs, especially in systemic amyloidosis.
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Written by
Urooj ArifUrooj is a skilled content writer at Ask Difference, known for her exceptional ability to simplify complex topics into engaging and informative content. With a passion for research and a flair for clear, concise writing, she consistently delivers articles that resonate with our diverse audience.
Edited by
Tayyaba RehmanTayyaba Rehman is a distinguished writer, currently serving as a primary contributor to askdifference.com. As a researcher in semantics and etymology, Tayyaba's passion for the complexity of languages and their distinctions has found a perfect home on the platform. Tayyaba delves into the intricacies of language, distinguishing between commonly confused words and phrases, thereby providing clarity for readers worldwide.
