Abstract
Prion diseases or transmissible spongiform encephalopathies (TSEs) are a family of rare progressive neurodegenerative disorders that affect both humans and animals. They are distinguished by long incubation periods, characteristic spongiform changes associated with neuronal loss, and a failure to induce inflammatory response. Prion diseases in animals, Scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (commonly known as "mad cow disease") in cattle, and Creutzfeldt-Jakob disease in humans are all examples of infectious diseases. The prion protein (PrP) was identified in a patient in 2015, and it was previously believed to be the cause of all known mammalian prion diseases. However, The protein alpha-synuclein, which is thought to be responsible for MSA, was suggested to be the cause of the disease in 2015.
Highlights
Prusiner is a term used to describe a tiny proteinaceous infectious particle that is resistant to most nucleic acid inactivation methods
The source of the abnormal three-dimensional structure is unknown, The name "prion" originates from the phrase "proteinaceous infectious particle," which means "proteinaceous infectious particle." When compared to other known infectious agents, such as virus-like organisms, bacteria and fungi, and parasites, the hypothesised role of protein as an infectious agent is in stark contrast to the other known infectious agents, which are all made up of nucleic acids and are incompatible with the hypothesis (DNA, RNA, or both).[2][3][4]
Scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy in cattle, and Creutzfeldt-Jakob disease in humans are all examples of infectious diseases. [6]
Summary
Prusiner is a term used to describe a tiny proteinaceous infectious particle that is resistant to most nucleic acid inactivation methods. In the case where the protein is produced by a normally suppressed gene and the protein's introduction has the ability to induce the gene's expression, thereby reawakening the dormant gene, the result would be a process indistinguishable from replication, because the gene's expression would produce the protein, which in turn would wake up the gene in other cells, as previously stated According to his second hypothesis, which serves as the foundation for contemporary prion theory, an abnormal form of a cellular protein could cause normal proteins of a similar kind to be converted into the abnormal form, resulting in the spread of the disease.
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