Phenotypic Similarity of Transmissible Mink Encephalopathy in Cattle and L-type Bovine Spongiform Encephalopathy in a Mouse Model

Baron, Thierry; Bencsik, Anna; Biacabe, Anne-Gaëlle; Morignat, Eric; Bessen, Richard A.

doi:10.3201/eid13112.070635

Cited by 33 publications

(57 citation statements)

References 32 publications

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“…Whereas the H-type is faithfully propagated in PrP VRQ transgenic mice [20], a new strain, converging to BSE appears on transmission of L-type BSE to these mice [21]. A different situation was observed in PrP ARQ mice: the H-type was not transmissible and the L-type agent was faithfully propagated [8]. (B) Variant CJD (vCJD) exhibits strain-specific traits undistinguishable from BSE on transmission to bovine and ovine (PrP VRQ ) transgenic mice, further comforting their etiological link [20,175].…”

Section: New Strains Can Emerge From Classical and Atypical Bse Agentsmentioning

confidence: 99%

“…3). Indeed, BSE propagates in PrP ARQ -mice without an obvious transmission barrier, the H-type is not transmissible and L-type isolates induce disease faster than BSE and retain their initial phenotype [8,20,21,59]. It remains to be clarified whether such a discrepant behaviour is indeed attributable to the PrP polymorphism at codon 136, or to the different genetic backgrounds and/or PrP constructs in the PrP ARQ and PrP VRQ mouse lines [60].…”

Section: Potential Of Interspecies Transmission Of Atypical Cattle Tsementioning

confidence: 99%

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Prion agent diversity and species barrier

2008

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-Mammalian prions are the infectious agents responsible for transmissible spongiform encephalopathies (TSE), a group of fatal, neurodegenerative diseases, affecting both domestic animals and humans. The most widely accepted view to date is that these agents lack a nucleic acid genome and consist primarily of PrP Sc , a misfolded, aggregated form of the host-encoded cellular prion protein (PrP C ) that propagates by autocatalytic conversion and accumulates mainly in the brain. The BSE epizooty, allied with the emergence of its human counterpart, variant CJD, has focused much attention on two characteristics that prions share with conventional infectious agents. First, the existence of multiple prion strains that impose, after inoculation in the same host, specific and stable phenotypic traits such as incubation period, molecular pattern of PrP Sc and neuropathology. Prion strains are thought to be enciphered within distinct PrP Sc conformers. Second, a transmission barrier exists that restricts the propagation of prions between different species. Here we discuss the possible situations resulting from the confrontation between species barrier and prion strain diversity, the molecular mechanisms involved and the potential of interspecies transmission of animal prions, including recently discovered forms of TSE in ruminants.prion / strain / misfolding / species barrier / PrP Table of Mammalian prion diseases or transmissible spongiform encephalopathies (TSE) form a group of related, invariably fatal neurodegenerative disorders of both animals and humans. The brain pathology consists of spongiosis, astrocytosis, neuronal loss and neural tissue from affected individuals contains an infectious agent, the prion, setting these diseases apart from other neurodegenerative diseases. Prion replication is thought to involve in essence the self-perpetuating conversion of the host-encoded cellular prion protein (PrP C ) into a misfolded form (PrP Sc ) that tends to aggregate and may be neurotoxic (for reviews [1,157]). Prion replication may also occur in lymphoid tissues but is there poorly if not pathogenic (for review [126], [133]). PrP C is a protein with two variably occupied glycosylation sites. It is attached at the outer of the plasma membrane by a glycosylphosphatidylinositol anchor. Its secondary structure is rich in alpha-helix and the protein is likely to be in a monomeric state in mild detergents. While its precise physiological function has not been assigned, PrP C is essential for prion replication and neurotoxicity to occur [57,129]. Upon infection, PrP C is refolded -without apparent post-translational modification -into beta-sheet -rich PrP Sc , initially in the presence of exogenous PrP Sc and then by an autocatalytic process. It leads to the formation of aggregates, sometimes of amyloid type, that can be differentiated from PrP C because of their partial resistance to protease digestion and of their insolubility into non-denaturing detergents [153]. Proteinase K, the most commonly used protease, di...

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Section: New Strains Can Emerge From Classical and Atypical Bse Agentsmentioning

confidence: 99%

Section: Potential Of Interspecies Transmission Of Atypical Cattle Tsementioning

confidence: 99%

Prion agent diversity and species barrier

2008

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“…In 1997, it was shown that transmission of BSE to transgenic mice was possible (Scott et al, 1997), and in 2006, transmission of BSE to wild-type mice was shown to be possible (Baron et al, 2006). Multiple mouse models have been developed to study prion diseases with different susceptibilities for bovine, sheep, mink, and porcine spongiform encephalopathy (Baron et al, 2007;Wilson et al, 2012). Additionally, fundamental research into prion diseases in mice (Telling, 2011) has contributed significantly to our understanding of the molecular mechanism and structure of prions as well as disease progression and transmission (Riek et al, 1996).…”

Section: Bovine Spongiform Encephalopathy (Bse)mentioning

confidence: 99%

Section: Bovine Spongiform Encephalopathy (Bse)mentioning

confidence: 99%

“…Known transmission vectors of the parasite include horseflies and vampire bats. Mouse models have been developed to study the infection routes and pathogenicity of Trypanosoma, reviewed by Antoine-Moussiaux et al (2008), Blom-Potar et al (2010), and Síma et al (2011). Mouse models have played an essential role in finding genetic loci underlying resistance or susceptibility to trypanosomiasis (Foote et al, 2005).…”

Section: Mouse As a Model For Animal Diseases 621 Trypanosomiasismentioning

confidence: 99%

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Invited review: Genetic and genomic mouse models for livestock research

2018

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Abstract. Knowledge about the function and functioning of single or multiple interacting genes is of the utmost significance for understanding the organism as a whole and for accurate livestock improvement through genomic selection. This includes, but is not limited to, understanding the ontogenetic and environmentally driven regulation of gene action contributing to simple and complex traits. Genetically modified mice, in which the functions of single genes are annotated; mice with reduced genetic complexity; and simplified structured populations are tools to gain fundamental knowledge of inheritance patterns and whole system genetics and genomics. In this review, we briefly describe existing mouse resources and discuss their value for fundamental and applied research in livestock.

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Animal Prion Diseases

Windl

Dawson

2012

Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease

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Prion diseases occur in many animal species, most notably in ruminants. While scrapie in sheep has been recognised for three centuries and goat scrapie has been recognised for decades, BSE in cattle is a relatively novel disease which was first diagnosed in the UK in the mid 1980s. BSE was most likely caused through dietary exposure to animal feed contaminated with prions and disease was subsequently transmitted to people. The BSE epidemic is almost at an end, but the recent identification of so called atypical forms of BSE and scrapie pose many questions about the possible spectrum of prion diseases in animals and their transmissibility to other species, including humans.The pathogenesis of animal prion diseases has been studied both in natural infections and in experimental animal models. Detection of infectivity is greatly helped by suitable rodent models, in particular transgenic mice. Clinically infected animals show characteristic neuropathology in the brain and spinal cord which is accompanied by the accumulation of a conformationally altered, protease-resistant host protein. The post-mortem diagnosis is based on the detection of this protein, PrP(Sc), but despite recent impressive developments a routine ante-mortem diagnostic test has proved elusive.There is no treatment for prion diseases in animals, but disease outbreaks are controlled through a mixture of movement restrictions on holdings, culling of affected animals and herds and, for classical scrapie in sheep, selective breeding for genetic resistance. Prions are very stable and can remain in the environment for prolonged periods. This poses serious practical questions with regard to the decontamination of infected premises. The control of BSE specifically through restrictions in animal feeding practises has been successful, but the changing spectrum of these diseases plus the economic pressures to relax feed bans and reduce levels of surveillance will require constant vigilance to safeguard animal and public health.

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Phenotypic Similarity of Transmissible Mink Encephalopathy in Cattle and L-type Bovine Spongiform Encephalopathy in a Mouse Model

Abstract: L-type BSE is a more likely candidate for the origin of TME than typical BSE.

Cited by 33 publications

References 32 publications

Prion agent diversity and species barrier

Prion agent diversity and species barrier

Invited review: Genetic and genomic mouse models for livestock research

Animal Prion Diseases

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