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Research Details

An Overview of Prion Diseases: Protein Transformation, Effects on Animals, and Current Treatments

An Overview of Prion Diseases: Protein Transformation, Effects on Animals, and Current Treatments

Prion disease is an extremely rare disease that occurs in about 1 in a million people, and people usually die in a couple of months to years following diagnosis. This disease predominantly affects the population older than 60, as the symptoms appear more frequently at this age. The distribution of this disease is completely random, and there is no specific area of distribution of this disease in the world except kuru. Kuru is in Papua New Guinea. However, the emergence of the prion disease occurs well before in the nervous system. There are cases of the prion disease occurring in other parts of the body, but it primarily develops in the nervous system. One single abnormal prion protein can transform the entire environment of the human body, and terrifyingly, it can be spontaneous. Although the disease is rare it is unpredictable, and anyone can have it. Especially with the abnormal prion protein’s resistance to “death”, there is no stopping once the first prion protein has transformed and seeded in the body. Without the complete knowledge of the prion disease and the mechanism that causes it in the first place, there is no absolute cure for this disease. The knowledge related to even knowing the complete mechanism and duty of the normal prion protein is unknown. What has been studied is that the gene responsible for the prion protein synthesis has been highly conserved in mammals, indicating an evolutionary importance. Nonetheless, other mammals are in danger of the prion disease. As more mutants of prion disease grow in animals, humans are more in danger of contracting it, such as the outbreak in England in 1986. Although this outbreak was not a large outbreak, people unfortunately fell victim to the disease. Furthermore, this predicts future epidemiological issues that can occur without a clear cure for prion disease.

 

By: Neha Katakamshetty

 

DOI Link: https://doi.org/10.47611/jsrhs.v12i4.5183