Prion diseases or transmissible spongiform encephalopathies.edited

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Prion Disease Analysis Name Institution Course Professor Date Name of the disease: Prion Disease Transmissible spongiform encephalopathies (TSEs), also referred to as prion diseases, are an uncommon group of progressive neurodegenerative conditions that impact both canines and felines. These entities are characterized by protracted incubation periods, discernible spongiform alterations corresponding to neuronal depletion, and an inability to elicit an inflammatory reaction. These illnesses are caused by an unconventional agent that lacks DNA or RNA, indicating that it did not come from a bacterial or viral source. This work aims to provide a comprehensive analysis of prion diseases, focusing particularly on the etiological agent. Prions are hypothesized to be the root cause of TSEs. The phrase "prions" denotes pathogenic, abnormal entities that are transmissible and possess the capability to trigger aberrant folding of normal cellular proteins named prion proteins. These proteins are particularly

abundant in the brain (Donaldson et al., 2016). Prion aggregates and clusters before they become visible under an electron microscope; they are considerably smaller than viruses. Furthermore, unlike bacteria, viruses, fungi, and other pathogens, prion systems lack nucleic acid. Alpha helices, which are flexible spirals, are believed to compose the normal prion protein (Baldwin et al., 2019). However, in its aberrantly folded state, these helices undergo significant stretching and elongation, resulting in the formation of densely packed beta sheets. Infected animals harbor prions in their brains, spinal columns, and lymph nodes. Additionally, these substances are present in considerably diminished concentrations in many other bodily fluids and tissues. Prion proteins are integral to cell adhesion and signaling and are on the cell membrane. Prions expelled by living animals in their excrement, urine, and saliva may stick to the soil and stay infectious. The categorization of prions is highly distinctive, and it is dubious whether they qualify as organisms. Due to its conformational alteration, prions are inapplicable to conventional classification schemes that include kingdom, domain, phylum, order, class, species, family, and genus. Virulence components of the pathogen are the capacity to invade and adhere to host cells. By binding particular receptors on the outermost layer of neurons and other cells, prion particles can be endocytosed into the cells.

Transmission Prions are distinctive in that they are proteinaceous entities devoid of nucleic acids and exhibit the characteristic of being Prion diseases exhibit a spectrum of transmissibility levels: CWD and scrapie, for instance, are highly contagious and easy to be transmitted among susceptible individuals; CJD and BSE, on the other hand, demonstrate minimal horizontal transmission and are transmitted through food. Kuru, identified in 1957, was the initial human prion disease to be determined to be transmissible. Infections are transmitted most frequently via direct intracerebral injection (Gough & Maddison, 2010). This is primarily the result of experimental inoculation. Iatrogenic transmission has transpired due to the unintentional use of electrodes on patients with undiagnosed CJD, which were subsequently rinsed with standard disinfectants prior to their application on other patients. Prions, which are pathogenic agents, can induce aberrant folding of prion proteins commonly found within the brain. The following symptoms characterize prion diseases:  • Dementia with a rapid onset of progression  • Hallucinations

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• Gait alterations and walking difficulties  • Muscle stiffness • Speech difficulties  • Confusion  • Fatigue Prion diseases can be established by providing brain tissue samples for biopsy or postmortem examination. Healthcare professionals may conduct various tests in advance to assist in the diagnosis of prion diseases like CJD or to exclude alternative conditions that present comparable symptoms. It is advisable to contemplate proton diseases in all individuals exhibiting rapidly progressive dementia. The diagnostic procedures encompass the following: • Brain scans using magnetic resonance imaging (MRI) • Blood tests • Spinal cord fluid samples (spinal tap, alternatively referred to as lumbar puncture)

• An EEG is a non-invasive method of analyzing brain waves that involves placing electrodes on the skull. • Neurological and visual examinations to detect nerve injury and vision impairment Although prion diseases are incurable, specific medications may be able to impede their progression. Despite the progressive and incapacitating symptoms, medical management of these conditions aims to maintain the safety and comfort of those affected. By sterilizing and cleansing medical equipment appropriately, the disease may be prevented from spreading. Reducing the number of regulations governing the feeding and management of cattle could impede the transmission of prion diseases. Human prion disorders affect 1-2 people per million people worldwide on an annual basis. Three categories can be used to group the conditions: acquired, hereditary, and spontaneous. The incidence rate increased to 1.4 per million in 2013 from 1.0 per million in 2004. According to the study, 5,212 persons worldwide suffer from prion disease (Maddox et al., 2020), with about 300 instances reported in the US each year. Maddox et al. (2020) discovered that 57% of the participants in their study died at that age. All of the deceased individuals were below the age of thirty. The average yearly incidence rate for this age group was 6.2 occurrences per billion. It is noteworthy to mention that sporadic instances of prion disease were assigned to only two of these cases. The annual incidence rate for individuals 65 and older was 5.9 per million on average. This condition predominantly impacts individuals within the age range of 50 to 75 years.

To summarize, Piron sickness demands significant attention due to its global impact and widespread effects. Although rare, Piron infections constitute a distinct and destructive group of infectious illnesses. Gaining knowledge of the causative organism, its attributes, and the mechanisms of transmission is crucial for effectively managing and preventing these disorders. This paper is an examination of the illness, including its symptoms and diagnostic techniques. References

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Baldwin, K. J., & Correll, C. M. (2019, August). Prion disease. In Seminars in Neurology (Vol. 39, No. 04, pp. 428–439). Thieme Medical Publishers. Gough, K. C., & Maddison, B. C. (2010). Prion transmission: prion excretion and occurrence in the environment. Prion, 4(4), 275-282. Donaldson, D. S., Sehgal, A., Rios, D., Williams, I. R., & Mabbott, N. A. (2016). Increased abundance of M cells in the gut epithelium dramatically enhances oral prion disease susceptibility. PloS Pathogens, 12(12), e1006075. Maddox, R. A., Person, M. K., Blevins, J. E., Abrams, J. Y., Appleby, B. S., Schonberger, L. B., & Belay, E. D. (2020). Prion disease incidence in the United States: 2003–2015. Neurology, 94(2), e153-e157.

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