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Salivary prions in sheep and deer.

Scrapie of sheep and chronic wasting disease (CWD) of cervids are transmissible prion diseases. Milk and placenta have been identified as sources of scrapie prions but do not explain horizontal transmission. In contrast, CWD prions have been reported in saliva, urine and feces, which are thought to be responsible for horizontal transmission. While the titers of CWD prions have been measured in feces, levels in saliva or urine are unknown. Because sheep produce ~17 L/day of saliva, and scrapie prions are present in tongue and salivary glands of infected sheep, we asked if scrapie prions are she…

Presymptomatic detection of prions in blood.

Prions are thought to be the proteinaceous infectious agents responsible for transmissible spongiform encephalopathies (TSEs). PrP(Sc), the main component of the infectious agent, is also the only validated surrogate marker for the disease, and its sensitive detection is critical for minimizing the spread of the disease. We detected PrP(Sc) biochemically in the blood of hamsters infected with scrapie during most of the presymptomatic phase of the disease. At early stages of the incubation period, PrP(Sc) detected in blood was likely to be from the peripheral replication of prions, whereas at t…

Prions: who should worry about them?

Prion diseases, also called transmissible spongiform encephalopathies (TSEs), are a family of neurodegenerative disorders affecting both humans and animals. They are caused by the accumulation of an abnormal form of a protein known as prion that results in neuronal death and a characteristic spongiform appearance of the brain tissue. Human prion diseases can be sporadic, acquired or hereditary. Acquired prion diseases have been linked to entering contaminated food into the human food chain, failure to completely disinfect or sterilize contaminated surgical instruments, patients receiving tissu

Prions: health scare and biological challenge.

Although human prion diseases are rare, the incidence of 'new variant' Creutzfeldt-Jakob disease in the United Kingdom is increasing exponentially. Given that this disease is probably the result of infection with bovine prions, understanding how prions replicate--and how to counteract their action--has become a central issue for public health. What are the links between the bovine and human prion diseases, and how do prions reach and damage the central nervous system?

Neurodegeneration in humans caused by prions.

Prion diseases include kuru, Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker disease, and fatal familial insomnia of humans as well as scrapie and bovine spongiform encephalopathy of animals. For many years, the prion diseases were thought to be caused by viruses despite evidence to the contrary. The unique characteristic common to all of these disorders, whether sporadic, dominantly inherited, or acquired by infection, is that they involve aberrant metabolism of the prion protein. In many cases, the cellular prion protein is converted into the scrapie variant by a process after tran

Kuru prions and sporadic Creutzfeldt-Jakob disease prions have equivalent transmission properties in transgenic and wild-type mice.

Kuru provides our principal experience of an epidemic human prion disease and primarily affected the Fore linguistic group of the Eastern Highlands of Papua New Guinea. Kuru was transmitted by the practice of consuming dead relatives as a mark of respect and mourning (transumption). To date, detailed information of the prion strain type propagated in kuru has been lacking. Here, we directly compare the transmission properties of kuru prions with sporadic, iatrogenic, and variant Creutzfeldt-Jakob disease (CJD) prions in Prnp-null transgenic mice expressing human prion protein and in wild-type …

Prion diseases and emerging prion diseases.

Transmissible spongiform encephalopathies (TSEs), also called prion diseases, are fatal neurodegenerative disorders. An abnormal isoform of the prion protein (PrP(Sc)) generated by post-translational modification of the cellular prion protein (PrP(C)) is believed to be the main component of this infectious agent. PrP(Sc) is relatively resistant to proteinase K (PK) digestion. This characteristic has been widely accepted as the physicochemical basis for distinguishing between PrP(C) and PrP(Sc). PrP(C) is a glycoprotein that contains 2 Asn-linked glycosylation sites; it is present in the cells

[The prion hypothesis and the human prion diseases].

Our understanding of the pathogenesis of the transmissible spongiform encephalopathies (TSE) has made terrific headway over the past 40 years and some scientists are even of the opinion that this group of diseases belongs to the neurodegenerative syndromes best understood. On the other hand, the investigation of TSE has led to a multitude of unexpected and surprising results and consequently has initiated impassioned discussions among scientists. Although the human forms of TSE are very rare, the wildfire-like spread of the bovine spongiform encephalopathy (BSE) raises the pressing question as

Prion Pathogenesis Revealed in a Series of the Special Issues "Prions and Prion Diseases".

Prion diseases are a group of devastating neurodegenerative disorders, which include Creutzfeldt-Jakob disease (CJD) in humans, and scrapie and bovine spongiform encephalopathy (BSE) in animals [...].

Immunomodulation for prion and prion-related diseases.

Prion diseases are a unique category of illness, affecting both animals and humans, where the underlying pathogenesis is related to a conformational change of a normal self protein called cellular prion protein to a pathological and infectious conformer known as scrapie prion protein (PrP(Sc)). Currently, all prion diseases lack effective treatment and are universally fatal. Past experiences with bovine spongiform encephalopathy and variant Creutzfeldt-Jakob disease mainly in Europe, as well as the current epidemic of chronic wasting disease in North America, have highlighted the need to devel

Aβ and Tau Prions Causing Alzheimer's Disease.

Studies show that patients with Alzheimer's disease (AD) have both Aβ and tau prions, and thus, AD is a double-prion disease. AD patients with the greatest longevity exhibited low levels of both Aβ and tau prions; tau prions were nearly absent in the brains of almost half of the patients who lived beyond 80 years of age. Using cellular bioassays for prions in postmortem samples, we found that both Aβ and tau proteins misfold into prions leading to AD, which is either a sporadic or familial dementing disorder. Although AD is transmissible experimentally, there is no evidence that AD is either c…

Microbial Prions: Dawn of a New Era.

Protein misfolding and aggregation are associated with human diseases and aging. However, microorganisms widely exploit the self-propagating properties of misfolded infectious protein particles, prions, as epigenetic information carriers that drive various phenotypic adaptations and encode molecular information. Microbial prion research has faced a paradigm shift in recent years, with breakthroughs that demonstrate the great functional and structural diversity of these agents. Here, we outline unorthodox examples of microbial prions in yeast and other microorganisms, focusing on their noncanon…

[Psychiatric manifestations by prions. A narrative review].

Prion diseases are a group of rare and rapidly progressive neurodegenerative conditions that may cause neuropsychiatric symptoms. This group … ed as idiopathic, inherited and acquired through exposure to exogenous material containing abnormal prions. The most prominent neurological manifestation of prion diseases is the emergence of a rapidly progressive dementia, mioclonus associated with cerebellar ataxia and also extra pyramidal symptoms. Psychiatric symptoms occur in early stages of the ill …

Amyloids or prions? That is the question.

Despite major efforts devoted to understanding the phenomenon of prion transmissibility, it is still poorly understood how this property is encoded in the amino acid sequence. In recent years, experimental data on yeast prion domains allow to start at least partially decrypting the sequence requirements of prion formation. These experiments illustrate the need for intrinsically disordered sequence regions enriched with a particularly high proportion of glutamine and asparagine. Bioinformatic analysis suggests that these regions strike a balance between sufficient amyloid nucleation propensity

Molecular barriers to zoonotic transmission of prions.

The risks posed to human health by individual animal prion diseases cannot be determined a priori and are difficult to address empirically. The fundamental event in prion disease pathogenesis is thought to be the seeded conversion of normal prion protein to its pathologic isoform. We used a rapid molecular conversion assay (protein misfolding cyclic amplification) to test whether brain homogenates from specimens of classical bovine spongiform encephalopathy (BSE), atypical BSE (H-type BSE and L-type BSE), classical scrapie, atypical scrapie, and chronic wasting disease can convert normal human

Основы прионов и их активация (обзор).

Прион — инфекционная частица, состоящая из аномальной изоформы прионного белка (PrPSc) и вызывающая такие прионские заболевания, как энцефалопатия говядины (BSE), болезнь Креуцфельда-Якоба (CJD) и скрепи. Принимающие клетки выражают клеточный прионный белок (PrPC), который играет роль в обычных функциях, таких как антиокисляющий стресс. PrPSc получается из ПХП и производится путем преобразования в конформацию. Прион известен как резистентный патоген, который трудно активировать с помощью обычных процедур стерилизации. Поэтому для предупреждения прионовых иатрогенных заболеваний важное значение

Совпадение в аннотации оригинала
Prion is an infectious particle composed of an abnormal isoform of the prion protein (PrPSc) and causes prion diseases such as bovine spongi … efore, to prevent prion-caused iatrogenic diseases, the use of appropriate procedures to inactivate prions is important. For examples, alcohol treatment, autoclave (121˚C, 20 min) and γ-ray irradiation, which are used for disinfection, antisepsis or sterilization of viruses and bacteria, are not effective against prion. This is a fundamental review of pr …