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The truth about transmissible spongiform encephalopathy: How does Prion sneak into our brains?
In the world of biology, the emergence of the term Prion symbolizes a brand-new disease transmission mechanism. Prion is an abnormally folded protein that has the ability to induce normal protein refolding, thereby triggering cell death. These diseases, known as transmissible spongiform encephalopathies (TSEs), are fatal and contagious neurodegenerative diseases in both humans and animals.
Prion's existence challenges our understanding of infectious diseases. It does not contain nucleic acids (DNA or RNA) like viruses, bacteria or fungi, but is composed solely of proteins. Prion is primarily a twisted isoform of the major prion protein (PrP), a protein that occurs naturally in organisms but whose role is still unclear.
"Prion can stably induce misfolding of other normal proteins through its specific three-dimensional structure."
Various TSEs in humans and other animals, including trafficking disease in sheep, chronic wasting disease in deer, spongiform encephalopathy in cattle (commonly known as mad cow disease), and Creutzfeldt-Jakob disease (CJD) in humans, are thought to be caused by the common Caused by misfolding of Lyon protein. From the perspective of the progression of these diseases, they are characterized by gradual progression, no effective treatment, and ultimately death.
Until 2015, scientists discovered that another form of prion called alpha-synuclein was associated with multiple system atrophy (MSA), completely overturning early understanding of prion disease. This means we may need to re-evaluate the association between prion and other neurodegenerative diseases, such as Alzheimer's and Parkinson's disease.
"Prion's structural stability makes it difficult to be degraded by chemical or physical factors, which poses challenges to the safety of medical devices."
The abnormally folded form of prion protein, PrPSc, converts normal PrPC into an infectious form. This characteristic of infectious prion allows it to continue to spread. These plastic needle-like aggregates cannot be degraded by normal biological enzymes and accumulate in brain tissue, causing cell damage and death, forming obvious pathological changes, including "cavitation" in brain tissue, making the tissue appear spongy. structure.
In general, prion disease has a relatively long incubation period, and after symptoms appear, the disease progresses rapidly, leading to brain damage and death. Various neurodegenerative symptoms including convulsions, dementia, ataxia, and behavioral or personality changes have been directly linked to prion transmission.
"According to research, prion can be absorbed into plants through the environment, further expanding its spread."
The biggest challenge in preventing the spread of pryon is its stability in the environment. Studies have shown that prion can enter the soil through the remains of corpses, urine, saliva and other body fluids, and remain in the environment for a long time. In addition, when plants grow in contaminated soil, these plants may also act as vectors for prion, further increasing the risk of its spread.
Although scientists have conducted many experiments to find effective attenuation and disinfection methods, they have not been able to completely eliminate the infectivity caused by Prion. This is an urgent health challenge for both patients and medical workers.
As we learn more about prion and how it spreads, we may be able to find new treatments and improve our ability to prevent and respond to these diseases. As we gradually understand how Prion cuts into the root of life, we can’t help but wonder: How can we effectively guard against these invisible enemies in future medical research?
