Prions: definition, examples, meaning, Structure, Topic
The topic of Prions covers a new class of disease-causing particles that are of recent biological knowledge. Unlike bacteria, viruses, or fungi, prions are non-nucleic acid, abnormally folded proteins which, however, can induce disease by encouraging misfolding of normal proteins, particularly in the brain and nervous system. They are also linked with lethal neurodegenerative diseases like Creutzfeldt-Jakob disease (CJD) in humans, Bovine Spongiform Encephalopathy (BSE or "mad cow disease") in cows, and scrapie in sheep. Prions are very resistant to regular sterilisation methods, which makes them difficult to eradicate and leads to serious issues in medical and food safety protocols.
- What Are Prions?
- Characteristics Of Prions
- Structure And Composition of Prions
- Difference between prions and other infectious agents (bacteria, viruses, fungi).
- Classification of Prions
- Disease-Causing Prions
- Mechanism of Disease Progression: Pathogenesis of Prion Diseases
- Treatment And Prevention
- Recommended Video on Viruses, Viroids and Prions
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Studies on prions have uncovered new knowledge on protein biology and neurodegeneration processes. These agents demonstrate how even inanimate species can disrupt normal physiological processes and lead to catastrophic, irreversible effects. Because prion diseases remain untreatable and always fatal, all efforts thus far have concentrated on early diagnosis, containment, and prevention. Research on prions also offers hints towards greater neurological diseases such as Alzheimer's and Parkinson's diseases, which may be caused by the same mechanisms of protein misfolding and aggregation.
What Are Prions?
Prions are infectious protein particles that have no genetic material like DNA or RNA. They are formed from the misfolding of a healthy cellular protein named prion protein (PrP), which is frequently present in the brain. After they misfold, prions trigger a chain reaction where other healthy PrP molecules become misfolded, leading to the development of clumps that destroy brain tissue. Prion diseases are severe but invariably fatal, and range from Creutzfeldt-Jakob Disease (CJD) in humans to Bovine Spongiform Encephalopathy (BSE) in cattle. Prion diseases are marked by lengthy incubation periods, the quick decline in mental function, and loss of motor function.
- Prions are infectious particles containing only protein, no nucleic acids.
- Induce fatal neurodegenerative illnesses in humans and animals.
- Causes brain damage due to protein misfolding and aggregation.
- Symptoms range from memory loss, coordination problems, and personality changes.
- Prion diseases are not amenable to normal disinfection and sterilisation procedures.
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Characteristics Of Prions
Prions are abnormally structured proteins with an unusual ability to replicate without genetic material, making them different from viruses, bacteria, and other pathogens. Their pathogenic form contains high concentrations of β-sheet structures, which render them insoluble and aggregative in neural tissues. Prions do not increase by reproduction but by changing the structure of normal proteins like themselves. They are species-restricted to a certain degree but can break species barriers in special conditions, resulting in new outbreaks. Their deposition results in spongiform encephalopathy in the brain, resulting in irreversible damage.
- Highly rich in β-sheet conformation, rendering them structurally stable and pathogenic.
- Multiply by structural conversion rather than reproduction.
- Demonstrate species barrier with occasional interspecies transmission.
- Accumulate in the neural tissue, resulting in spongiform degeneration.
- Fail to induce inflammation or an immune response during infection.
Structure And Composition of Prions
Prions are infectious entities that are made up of only misfolded protein, with no nucleic acids present, distinguishing them from viruses and bacteria. The misfolded proteins, scrapie prion proteins (PrP^Sc), are conformational isomers of the normal cellular prion proteins (PrP^C). The major structural difference is in the high number of β-sheet structures found in PrP^Sc, in place of the α-helices found in the normal form. This conformational alteration enables prions to cause the misfolding of normal proteins to the pathologic form, leading to a chain reaction. Prions are also extremely resistant to proteases, thus, they are very stable and long-lived in biological environments.
- Prions have no DNA or RNA—just protein.
- Disease-causing form (PrP^Sc) contains β-sheets rather than α-helices.
- Can transform normal proteins into abnormal, infectious versions.
- Extremely resistant to protease enzymes and environmental degradation.
- Able to spread and concentrate in tissues without provoking an immune response.
A diagram showing normal and misfolded protein in Prion.
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Difference between prions and other infectious agents (bacteria, viruses, fungi).
Feature | Prions | Bacteria | Viruses | Fungi |
Nature | Protein only (misfolded prion protein) | Single-celled microorganisms | Acellular particles with genetic material (DNA or RNA) | Eukaryotic organisms (single-celled or multicelled) |
Genetic Material | None | DNA | DNA or RNA | DNA |
Size | Extremely small | Larger than viruses; typically 0.2-2.0 µm | Smaller than bacteria; typically 20-300 nm | Larger than bacteria; variable sizes |
Cellular Structure | None | Prokaryotic cell structure | No cellular structure (acellular) | Eukaryotic cell structure |
Reproduction | Induces misfolding of normal proteins | Binary fission | Requires host cell machinery to replicate | Spore formation, budding, or binary fission |
Pathogenic Mechanism | Protein misfolding and aggregation | Toxins, invasion, and immune response | Hijacks host cell machinery for replication | Tissue invasion, toxin production |
Examples of Diseases | Creutzfeldt-Jakob disease (CJD), Bovine spongiform encephalopathy (BSE) | Tuberculosis, Streptococcal infections | Influenza, HIV/AIDS, COVID-19 | Athlete's foot, Candidiasis, Ringworm |
Treatment | No known cure; symptomatic relief only | Antibiotics | Antiviral drugs, vaccines | Antifungal drugs |
Resistance to Environmental Factors | Highly resistant to heat, UV radiation, and disinfectants | Variable, some form of spores | Generally sensitive to heat and disinfectants | Various spores can be highly resistant |
Classification of Prions
Prion diseases can be classified based on their origin. All of them are discussed below in the table:
| Type | Description | Examples | Prevalence |
|---|---|---|---|
| Sporadic | Occur unpredictably with no identifiable cause or genetic trait. | Sporadic Creutzfeldt-Jakob Disease (sCJD) | ~85% of all prion disease cases |
| Familial | Result from inherited mutations in the PRNP gene affecting the prion protein. | Familial CJD, Gerstmann-Sträussler-Scheinker Syndrome (GSS), Fatal Familial Insomnia (FFI) | 10–15% of all prion disease cases |
| Acquired | Caused by external infection via contaminated food, surgical tools, or cultural practices. | Variant CJD (vCJD), Kuru, Iatrogenic CJD (from surgeries, transplants, etc.) | Rare but infectious and serious |
Disease-Causing Prions
Some diseases caused by prions are:
| Disease | Description | Transmission | Symptoms / Impact |
|---|---|---|---|
| Creutzfeldt-Jakob Disease (CJD) | Human prion disease with progressive and fatal neurodegeneration. |
| Rapid mental decline, loss of coordination, fatal within months |
| Kuru | A neurodegenerative disease observed among the Fore people of Papua New Guinea | Ritualistic cannibalism, especially the consumption of the brain tissue of the deceased | Tremors, loss of balance, progressive brain damage |
| Bovine Spongiform Encephalopathy (BSE) | Affects cattle, causing sponge-like degeneration of brain tissue | Consumption of contaminated animal feed | Loss of coordination, behavioural changes, transmissible to humans as vCJD |
| Chronic Wasting Disease (CWD) | Affects deer, elk, and moose | Contact with infected body fluids or contaminated surfaces | Weight loss, abnormal behaviour,and brain degeneration |
Mechanism of Disease Progression: Pathogenesis of Prion Diseases
The diseases include Creutzfeldt-Jakob Disease, Gerstmann-Sträussler-Scheinker Syndrome, and many others are neurological disorders which are due to the abnormal post-transformation of normal cell surface prion proteins (PrP^C) into abnormal cell surface proteins (PrP^Sc). PrP^Sc is resistant to proteases and preferentially accumulates in an insoluble form, which is the form of insoluble fibrils. These fibrils build up in the brain, upsetting the normal functioning of neurons and causing neurodegeneration.
Impact on the Nervous System
Some major impact of prions on the human nervous system is discussed below:
| Effect | Description |
|---|---|
| Neuronal Damage | Accumulation of PrP^Sc causes degeneration in brain areas responsible for memory, movement, and balance. |
| Spongiform Changes | Brain tissue develops a sponge-like appearance due to vacuolation and neuron death. |
| Inflammatory Response | Prions activate microglia and astrocytes, causing neuroinflammation without triggering a classical immune response. |
Treatment And Prevention
Methods that can be adapted to prevent the diseases are:
| Category | Strategy | Description |
|---|---|---|
| Current Treatment | Symptomatic Relief | Managing symptoms such as pain, anxiety, and other general discomforts. |
| Supportive Care | Providing comfort-focused care to enhance patient quality of life. | |
| Experimental Therapies | Research on drugs aimed at controlling prion replication and preventing protein misfolding. | |
| Prevention | Food Safety | Laws and regulations to prevent transmission through contaminated meat products. |
| Screening | Testing blood and tissues to reduce the risks of transmission during medical procedures. | |
| Decontamination | Protocols for sterilising medical instruments and equipment to prevent the spread. | |
| Education | Increasing awareness about prion diseases and their risks among the public and healthcare workers. |
Recommended Video on Viruses, Viroids and Prions
Frequently Asked Questions (FAQs)
The prions are the pathogen that transmits diseases through a process that leads to the conversion of normal cell prion proteins, PrP^C into an abnormal form known as PrP^Sc. As noted above, these abnormal prions deposit at the synapses of the brain and cause neuronal damage, spongiform changes and consequently neurodegeneration, which is a hallmark of diseases by prions or Transmissible Spongiform Encephalopathies (TSE).
Some of the symptoms of the prion disease may be rapid memory loss or confusion, behavioural changes like anxiety or depression, difficulty in movement, tremors, late-stage dementia, and poor coordination.
Diagnosis of prion diseases is clinical as supported by imaging and laboratory investigations which may include imaging studies such as MRI and lab tests which may detect abnormal prion proteins in the cerebrospinal fluid or biopsy specimens. Subsequently, the definitive diagnosis is reserved, when by histological examination of the brain tissue typical spongiform changes and prion protein deposition are seen in the post-mortem examination.
As of now, there is still no way to eliminate or cure prion diseases, though various medications are being developed to counter them. Management is mainly on manifestations management, patient support and experimental treatment that is oriented at trying to slow down the disease process. Prion diseases do not have a cure and are typically lethal; however, the management focuses mainly on enhancing the patient’s quality of life.
Prevention of prion diseases includes:
Measures to control the spread of the disease through the incorporation of stiff measures that curtail spreading through meat products, especially from infected cattle affected with BSE.
Elimination of blood transfusions and transplantations so that the risk of spreading the disease through transplantation is averted.
Coming up with reasonable procedures to follow to clean medical equipment and areas where prion is likely to be present.
Raising the knowledge level of the public and the healthcare providers concerning prion diseases and their risks.
Prions consist mainly of misfolded proteins, particularly the prion protein (PrP), which can induce normal proteins in the brain to misfold, leading to neurodegenerative diseases. Unlike viruses or bacteria, prions contain no genetic material (DNA or RNA).
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