The prion is a terminal disease whose implications are caused by the variant degree of aggregations; thus the emergence of the various types of related diseases mainly the protein misfolding disorders and the prion diseases. According to Scheckel and Aguzzi (2018) in the research article about prion, they postulate that it is one of the illnesses that rarely occurs especially in human beings and only two scenarios mainly occur in a year. The agent of the disease is encephalopathies whose form is usually in sponge structure although it poses a high risk of transmitting from one being to another. The researchers further argue that although the PrP is the causative agent, it is quite a different case for the PMD. This is because amyloids cause PMD.
The success of the spread of the prion disease in the body is entangled in the reproduction process that involves the method of forming fragments from the nuclear cells. The PrD is a resistant element within the body since it has defence mechanisms against attacks from temperature variations as well as from other forms of the protein aggregates such as the proteases (Hu et al., 2016). This enhances the capacity of the prion disease to withstand harsh conditions of resistance as well as the adaptability capacity. Although the disease shows an exhilarating resistance from the environmental conditions, it is on the other hand, an architect of its destruction since it is dependent on the presence and enrichment of the PrP for successful reproduction system as well as the ability of its toxic levels to the body organs. The success of the interdependence within the functionality of the prion disease determines its effects in the body of the animal.
Ideally, the similarity index between the Prion and the protein misfolding disorder (PMD) is a lethal blend of causing deterioration of the healthy levels of the body cells. The PMD commonly relates to such diseases that involve the disruptions of the internal structures and functionalities of the cells such as the cancer cells as well as the Alzheimer disease. In most cases, the PMD contains the prionoids whose nature of transmissibility is on the lower scale and almost impossible apart from the individual cases of genetic inheritance with the single unit of the PMD being a propagon. This is a form of a disease that mostly affects the brain cells thus the relativity to the brain related illnesses due to the deterioration effects of the brain cells rendered from the spread of the propagon (Wulf, Senatore & Aguzzi, 2017). The significant difference from Prion is that its single unit, that is, propagon is of primary structure than that of the prion and becomes a prion once it successfully transmits to another cell after the replication.
In conclusion, this article is a focal point of underpinning the nature of some of the diseases through the Prion disease study. Majority of the cellular diseases prove difficult to be identified, and to some extent, the patients are misdiagnosed due to the rare occurrences of certain conditions. Some of the diseases that are easy to identify with include neurodegenerative diseases. As a knowledge pool, it has utilised previous research materials to stipulate that as much as the prion diseases exist, they are a severe infection to the functionality of the human bodies mainly because of their capacity to transmit, present persistence resistance to treatment while causing adverse effects through their increased levels of toxicity.
Hu, P. P., Morales, R., Duran-Aniotz, C., Moreno-Gonzalez, I., Khan, U., & Soto, C. (2016). Role of prion replication in the strain-dependent brain regional distribution of prions. Journal of Biological Chemistry, 291(24), 12880-12887.
Scheckel, C., & Aguzzi, A. (2018). Prions, prionoids and protein misfolding disorders. Nature Reviews Genetics, 1.
Wulf, M. A., Senatore, A., & Aguzzi, A. (2017). The biological function of the cellular prion protein: an update. BMC biology, 15(1), 34.