Prion in the context of Amyloid


Prion in the context of Amyloid

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⭐ Core Definition: Prion

A prion (/ˈprɒn/ ) is a misfolded protein that induces misfolding in normal variants of the same protein, leading to cellular death. Prions are responsible for prion diseases, known as transmissible spongiform encephalopathy (TSEs), which are fatal and transmissible neurodegenerative diseases affecting both humans and animals. These proteins can misfold sporadically, due to genetic mutations, or by exposure to an already misfolded protein, leading to an abnormal three-dimensional structure that can propagate misfolding in other proteins.

The term prion comes from "proteinaceous infectious particle". Unlike other infectious agents such as viruses, bacteria, and fungi, prions do not contain nucleic acids (DNA or RNA). Prions are mainly twisted isoforms of the major prion protein (PrP), a naturally occurring protein with an uncertain function. They are the hypothesized cause of various TSEs, including scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (BSE) in cattle (mad cow disease), and Creutzfeldt–Jakob disease (CJD) in humans.

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Prion in the context of Self-replication

Self-replication is any behavior of a dynamical system that yields construction of an identical or similar copy of itself. Biological cells, given suitable environments, reproduce by cell division. During cell division, DNA is replicated and can be transmitted to offspring during reproduction. Biological viruses can replicate, but only by commandeering the reproductive machinery of cells through a process of infection. Harmful prion proteins can replicate by converting normal proteins into rogue forms. Computer viruses reproduce using the hardware and software already present on computers. Self-replication in robotics has been an area of research and a subject of interest in science fiction. Any self-replicating mechanism which does not make a perfect copy (mutation) will experience genetic variation and will create variants of itself. These variants will be subject to natural selection, since some will be better at surviving in their current environment than others and will out-breed them.

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Prion in the context of Pathogen

In biology, a pathogen (Greek: πάθος, pathos "suffering", "passion" and -γενής, -genēs "producer of"), in the oldest and broadest sense, is any organism or agent that can produce disease. A pathogen may also be referred to as an infectious agent, or simply a germ.

The term pathogen came into use in the 1880s. Typically, the term pathogen is used to describe an infectious microorganism or agent, such as a virus, bacterium, protozoan, prion, viroid, or fungus. Small animals, such as helminths and insects, can also cause or transmit disease. However, these animals are usually referred to as parasites rather than pathogens. The scientific study of microscopic organisms, including microscopic pathogenic organisms, is called microbiology, while parasitology refers to the scientific study of parasites and the organisms that host them.

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Prion in the context of Zoonosis

A zoonosis (/zˈɒnəsɪs, ˌzəˈnsɪs/ ; plural zoonoses) or zoonotic disease is an infectious disease of humans caused by a pathogen (an infectious agent, such as a virus, bacterium, parasite, fungi, or prion) that can jump from a non-human vertebrate to a human. When humans infect non-humans, it is called reverse zoonosis or anthroponosis.

Major modern diseases such as Ebola and salmonellosis are zoonoses. HIV was a zoonotic disease transmitted to humans in the early part of the 20th century, though it has now evolved into a separate human-only disease. Human infection with animal influenza viruses is rare, as they do not transmit easily to or among humans. However, avian and swine influenza viruses in particular possess high zoonotic potential, and these occasionally recombine with human strains of the flu and can cause pandemics such as the 2009 swine flu. Zoonoses can be caused by a range of disease pathogens such as emergent viruses, bacteria, fungi and parasites; of 1,415 pathogens known to infect humans, 61% were zoonotic. Most human diseases originated in non-humans; however, only diseases that routinely involve non-human to human transmission, such as rabies, are considered direct zoonoses.

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Prion in the context of Medical microbiology

Medical microbiology, the large subset of microbiology that is applied to medicine, is a branch of medical science concerned with the prevention, diagnosis and treatment of infectious diseases. In addition, this field of science studies various clinical applications of microbes for the improvement of health. There are four kinds of microorganisms that cause infectious disease: bacteria, fungi, parasites and viruses, and one type of infectious protein called prion.

A medical microbiologist studies the characteristics of pathogens, their modes of transmission, mechanisms of infection and growth. The academic qualification as a clinical/Medical Microbiologist in a hospital or medical research centre generally requires a Bachelors degree while in some countries a Masters in Microbiology along with Ph.D. in any of the life-sciences (Biochem, Micro, Biotech, Genetics, etc.). Medical microbiologists often serve as consultants for physicians, providing identification of pathogens and suggesting treatment options. Using this information, a treatment can be devised.Other tasks may include the identification of potential health risks to the community or monitoring the evolution of potentially virulent or resistant strains of microbes, educating the community and assisting in the design of health practices. They may also assist in preventing or controlling epidemics and outbreaks of disease.Not all medical microbiologists study microbial pathology; some study common, non-pathogenic species to determine whether their properties can be used to develop antibiotics or other treatment methods.

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Prion in the context of Human pathogen

A human pathogen is a pathogen (microbe or microorganism such as a virus, bacterium, prion, or fungus) that causes disease in humans.

The human physiological defense against common pathogens (such as Pneumocystis) is mainly the responsibility of the immune system with help by some of the body's normal microbiota. However, if the immune system or "good" microbiota are damaged in any way (such as by chemotherapy, human immunodeficiency virus (HIV), or antibiotics being taken to kill other pathogens), pathogenic bacteria that were being held at bay can proliferate and cause harm to the host. Such cases are called opportunistic infections.

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Prion in the context of Proteinopathy

In medicine, proteinopathy ([pref. protein]; -pathy [suff. disease]; proteinopathies pl.; proteinopathic adj), or proteopathy, protein conformational disorder, or protein misfolding disease, is a class of diseases in which certain proteins become structurally abnormal, and thereby disrupt the function of cells, tissues and organs of the body.

Often the proteins fail to fold into their normal configuration; in this misfolded state, the proteins can become toxic in some way (a toxic gain-of-function) or they can lose their normal function. The proteinopathies include such diseases as Creutzfeldt–Jakob disease (and a variant associated with mad cow disease) and other prion diseases, Alzheimer's disease, Parkinson's disease, amyloidosis, multiple system atrophy, and a wide range of other disorders. The term proteopathy was first proposed in 2000 by Lary Walker and Harry LeVine.

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Prion in the context of Protein aggregation

In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease.

After synthesis, proteins typically fold into a particular three-dimensional conformation that is the most thermodynamically favorable: their native state. This folding process is driven by the hydrophobic effect: a tendency for hydrophobic (water-fearing) portions of the protein to shield themselves from the hydrophilic (water-loving) environment of the cell by burying into the interior of the protein. Thus, the exterior of a protein is typically hydrophilic, whereas the interior is typically hydrophobic.

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Prion in the context of Prion diseases

Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of progressive, incurable, and invariably fatal conditions that are associated with the degeneration of the nervous system in many animals, including humans, cattle, and sheep. Strong evidence supports the once unorthodox hypothesis that prion diseases are transmitted by abnormally shaped protein molecules known as prions. Prions consist of a protein called the prion protein (PrP). Misshapen PrP (often referred to as PrP) conveys its abnormal structure to naive PrP molecules by a crystallization-like seeding process. Because the abnormal proteins stick to each other, and because PrP is continuously produced by cells, PrP accumulates in the brain, harming neurons and eventually causing clinical disease.

Prion diseases are marked by mental and physical deterioration that worsens over time. A defining pathologic characteristic of prion diseases is the appearance of small vacuoles in various parts of the central nervous system that create a sponge-like appearance when brain tissue obtained at autopsy is examined under a microscope. Other changes in affected regions include the buildup of PrP, gliosis, and the loss of neurons.

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Prion in the context of Mad cow disease

Bovine spongiform encephalopathy (BSE), commonly known as mad cow disease, is an incurable and always fatal neurodegenerative disease of cattle. Symptoms include abnormal behavior, trouble walking, and weight loss. Later in the course of the disease, the cow becomes unable to function normally. There is conflicting information about the time between infection and onset of symptoms. In 2002, the World Health Organization suggested it to be approximately four to five years. Time from onset of symptoms to death is generally weeks to months. Spread to humans is believed to result in variant Creutzfeldt–Jakob disease (vCJD) or Creutzfeldt–Jakob disease (CJD). As of 2024, a total of 233 cases of vCJD had been reported globally.

BSE is thought to occur due to an infection by a misfolded protein, known as a prion. Cattle are believed to have been infected by being fed meat-and-bone meal that contained either the remains of cattle who spontaneously developed the disease or scrapie-infected sheep products. The United Kingdom was afflicted with an outbreak of BSE and vCJD in the 1980s and 1990s. The outbreak increased throughout the UK due to the practice of feeding meat-and-bone meal to young calves of dairy cows. Cases are suspected based on symptoms and confirmed by examination of the brain. Cases are classified as classic or atypical, with the latter divided into H- and L types. It is a type of transmissible spongiform encephalopathy.

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Prion in the context of Sterilization (microbiology)

Sterilization (British English: sterilisation) refers to any process that removes, kills, or deactivates all forms of life (particularly microorganisms such as fungi, bacteria, spores, and unicellular eukaryotic organisms) and other biological agents (such as prions or viruses) present in fluid or on a specific surface or object. Sterilization can be achieved through various means, including heat, chemicals, irradiation, high pressure, and filtration. Sterilization is distinct from disinfection, sanitization, and pasteurization, in that those methods reduce rather than eliminate all forms of life and biological agents present. After sterilization, fluid or an object is referred to as being sterile or aseptic.

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Prion in the context of Prion disease

Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of progressive, incurable, and invariably fatal conditions that are associated with the degeneration of the nervous system in many animals, including humans, cattle, and sheep. Strong evidence supports the once unorthodox hypothesis that prion diseases are transmitted by abnormally shaped protein molecules known as prions. Prions consist of a protein called the prion protein (PrP). Misshapen PrP (often referred to as PrP) conveys its abnormal structure to native PrP molecules by a crystallization-like seeding process. Because the abnormal proteins stick to each other, and because PrP is continuously produced by cells, PrP accumulates in the brain, harming neurons and eventually causing clinical disease.

Prion diseases are marked by mental and physical deterioration that worsens over time. A defining pathologic characteristic of prion diseases is the appearance of small vacuoles in various parts of the central nervous system that create a sponge-like appearance when brain tissue obtained at autopsy is examined under a microscope. Other changes in affected regions include the buildup of PrP, gliosis, and the loss of neurons.

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