The role of the immune system in prion infection

Mabbott, Neil A.; Alibhai, James; Manson, Jean

doi:10.1016/b978-0-444-63945-5.00005-2

Cited by 15 publications

(18 citation statements)

References 266 publications

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“…However, it was also noticed early on that the lymphoreticular system was not the only possible route for prions to reach the CNS [116]. Since then, the ability of prions to replicate in lymphoid tissues and their role on systemic prion propagation in the case of peripheral infections, especially in oral infections, has been extensively investigated [117,118]. In short, after oral exposure in the case of naturally transmitted scrapie, CWD, BSE, and vCJD, prions arrive to the small intestine and accumulate in gut-associated lymphoid tissues (GALT), such as Peyer's patches or other lymphoid organs such as tonsil.…”

Section: Detection Of Prp Sc In the Lymphoreticular Systemmentioning

confidence: 99%

“…In the previous sections it has been clearly established that despite being pathologies of the CNS, prions can replicate in extraneural tissues (such as lymphoid organs) and that they can spread to different locations through the peripheral nervous system [118,266]. Moreover, intraocular inoculations done to study the neural spread of prions [267] and the report of iatrogenic CJD cases due corneal transplants [268] clearly demonstrated that prions could spread in both directions along the axons.…”

Section: Detection Of Prp Sc In Olfactory Mucosamentioning

confidence: 99%

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Detection of Pathognomonic Biomarker PrPSc and the Contribution of Cell Free-Amplification Techniques to the Diagnosis of Prion Diseases

et al. 2020

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Transmissible spongiform encephalopathies or prion diseases are rapidly progressive neurodegenerative diseases, the clinical manifestation of which can resemble other promptly evolving neurological maladies. Therefore, the unequivocal ante-mortem diagnosis is highly challenging and was only possible by histopathological and immunohistochemical analysis of the brain at necropsy. Although surrogate biomarkers of neurological damage have become invaluable to complement clinical data and provide more accurate diagnostics at early stages, other neurodegenerative diseases show similar alterations hindering the differential diagnosis. To solve that, the detection of the pathognomonic biomarker of disease, PrP Sc , the aberrantly folded isoform of the prion protein, could be used. However, the amounts in easily accessible tissues or body fluids at pre-clinical or early clinical stages are extremely low for the standard detection methods. The solution comes from the recent development of in vitro prion propagation techniques, such as Protein Misfolding Cyclic Amplification (PMCA) and Real Time-Quaking Induced Conversion (RT-QuIC), which have been already applied to detect minute amounts of PrP Sc in different matrixes and make early diagnosis of prion diseases feasible in a near future. Herein, the most relevant tissues and body fluids in which PrP Sc has been detected in animals and humans are being reviewed, especially those in which cell-free prion propagation systems have been used with diagnostic purposes.

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Section: Detection Of Prp Sc In the Lymphoreticular Systemmentioning

confidence: 99%

Section: Detection Of Prp Sc In Olfactory Mucosamentioning

confidence: 99%

Detection of Pathognomonic Biomarker PrPSc and the Contribution of Cell Free-Amplification Techniques to the Diagnosis of Prion Diseases

et al. 2020

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“…They can also trap prions expressed by other infected cells, such as neurons. PrP Sc replication in the stromal compartment of the spleen occurs exclusively in PrP C ‐expressing FDCs; in other words, the pathology of prion diseases in SLOs is dependent on PrP C expression. A PrP C ‐deficient model established using the Cre‐LoxP recombinase system confirmed that PRNP deletion did not impact FDC maturation, the binding of immune complexes, or the maintenance of B lymphocyte affinity maturation in the GC.…”

Section: Functions Of Prpc In the Innate Immune Responsementioning

confidence: 99%

“…Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are chronically neurodegenerative and potentially zoonotic pathological processes. 1 The prototypic prion disease was first detected in sheep called "Scrapie" whose pathogen was called scrapie PrP (PrP Sc ). 2 Human TSEs include Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker disease, Kuru disease and fatal familial insomnia, among which CJD is most common.…”

Section: Introductionmentioning

confidence: 99%

Expression and functions of cellular prion proteins in immunocytes

et al. 2019

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Prion diseases are fatal neurodegenerative processes caused by the accumulation of the pathological prion protein, PrPSc. While pathological lesions are limited to the central nervous system (CNS), disease‐specific proteins accumulate and replicate in secondary lymphoid organs prior to neuroinvasion, and their replication there depends on the abundance of cellular prion protein (PrPC). PrPC is expressed in both central and peripheral lymphoid tissues, and up‐ or downregulates innate and adaptive immune responses. In addition to prion diseases, PrPC is also immunologically involved in other neurological disorders and infectious diseases, including Alzheimer's disease and human immunodeficiency virus infection. Herein, we summarize the expression and functions of PrPC in various immunocytes, as well as its immunological and pathological roles in neurodegeneration and infection.

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“…A study by Wyckoff et al [142] mentions the binding of prions to certain types of soil particles that may result in an increased uptake of prions from the gut lumen, but it is not yet clear if this uptake is mediated by M cells. Host infection by M-cell-independent mechanisms cannot be disregarded, namely, those involving directly enterocytes from the follicle-associated epithelium [143] or other M-cellindependent pathways [144].…”

Section: Cellsmentioning

confidence: 99%

TSE Monitoring in Wildlife Epidemiology, Transmission, Diagnosis, Genetics and Control

Machado¹,

Orge²,

Pires³

et al. 2019

Wildlife Population Monitoring

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Among the transmissible spongiform encephalopathies (TSEs), chronic wasting disease (CWD) in cervids is now the rising concern within Europe. CWD will be outlined in this chapter gathering its epidemiology, transmission, diagnosis, genetics, and control. Prion diseases are fatal neurodegenerative diseases characterized by the accumulation of an abnormal isoform of the prion protein (PrP c), usually designated by PrP sc or prion. CWD is a prion disease of natural transmission affecting cervids detected mainly in North America. The first European case was detected in Norway, in 2016, in a wild reindeer; until April 2018, a total of 23 cases were described. The definite diagnosis is postmortem, performed in target areas of the brain and lymph nodes. Samples are first screened using a rapid test and, if positive, confirmed by immunohistochemistry and Western immunoblotting. It is not possible to establish a culling plan based on the genotype, once affected animals appear with all genotypes. However, some polymorphisms seem to result in longer incubation periods or confer a reduced risk. The control is not easy in captive cervids and even more in the wildlife; some recommendations have been proposed in order to understand the danger and impact of CWD on animal and public health.

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The role of the immune system in prion infection

Cited by 15 publications

References 266 publications

Detection of Pathognomonic Biomarker PrPSc and the Contribution of Cell Free-Amplification Techniques to the Diagnosis of Prion Diseases

Detection of Pathognomonic Biomarker PrPSc and the Contribution of Cell Free-Amplification Techniques to the Diagnosis of Prion Diseases

Expression and functions of cellular prion proteins in immunocytes

TSE Monitoring in Wildlife Epidemiology, Transmission, Diagnosis, Genetics and Control

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