Conversion of the BASE Prion Strain into the BSE Strain: The Origin of BSE?

Capobianco, Raffaella; Casalone, Cristina; Suardi, Silvia; Mangieri, Michela; Miccolo, Claudia; Limido, Lucia; Catania, Marcella; Rossi, Giacomina; Fede, Giuseppe Di; Giaccone, Giorgio; Bruzzone, Maria Grazia; Minati, Ludovico; Corona, Cristiano; Acutis, Pier Luigi; Gelmetti, Daniela; Lombardi, Giovanna; Groschup, Martin H.; Buschmann, A.; Zanusso, Gianluigi; Monaco, Salvatore; Caramelli, Maria; Tagliavini, Fabrizio

doi:10.1371/journal.ppat.0030031

Cited by 151 publications

(187 citation statements)

References 36 publications

(53 reference statements)

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Section: Conservation Of Strain Phenotypementioning

confidence: 82%

“…Primary transmission of an Italian BSE-L case (termed BASE, for bovine amyloidogenic spongiform encephalopathy) to a panel of inbred mouse lines did not induce any clinical disease, nor PrP res accumulation. On secondary transmission however, a proportion of mice developed a disease with phenotypic traits undistinguishable from the BSE agent that has followed the same transmission history [45]. Intriguingly, transmission of BASE and three French L-type isolates to mice expressing ovine PrP (VRQ allele) also produced a shift towards a strain biochemically and neuropathologically undistinguishable from BSE, in this case from the primary passage on [21].…”

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

confidence: 98%

“…L-type PrP res molecules differed from zoonotic BSE by a They are associated with zoonotic ('classical') BSE cases and uncommon ('atypical') BSE cases (Ltype or H-type). These agents maintain distinct properties on serial passage in mice transgenic for bovine PrP (Bov) supporting the existence of at least three distinct prion strains in cattle [21,42,45]. Their potential of interspecies transmission has been assessed with transgenic mice expressing sheep VRQ (Ov VRQ ) or ARQ allele (Ov ARQ ) or human (MM allele, Hu Met ) PrP.…”

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

confidence: 99%

“…This was an important observation since it suggests that other loci than PrP might influence not only the susceptibility [124,136] but also the strain evolution. Puzzlingly, however, these results have not been reproduced in another study using a similar panel of inbred mice and different BSE isolates [45].More recently, Espinosa et al revisited BSE agent stability after passage through sheep species [73]. The transmission features were compared with cattle BSE in mice transgenic for bovine PrP [48].…”

mentioning

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: Conservation Of Strain Phenotypementioning

confidence: 82%

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

confidence: 98%

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

confidence: 99%

mentioning

confidence: 99%

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Prion agent diversity and species barrier

2008

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“…Another publication describes the transmission of a new bovine prion strain called bovine amyloidotic spongiform encephalopathy (BASE), which can be discriminated from BSE mainly on the basis of a lower molecular mass of the unglycosylated form of PrP D , a different anatomical distribution of the accumulated PrP D in the brain, and by the presence of PrP immunoreactive amyloid plaques, bovine PrP transgenic mice. Surprisingly, passage of this strain in conventional mice produced PrP D of the BSE phenotype, while bovine PrP transgenic mice revealed the PrP D signature of the BASE type [24]. Moreover, in a similar study, BASE prions acquired strain features closely similar to those of BSEtype agents when propagated in mice expressing ovine PrP (Tg338), although they retained the BASE-associated phenotypic traits in other lines, including bovine PrP mice [7].…”

Section: Phenotypic And/or Biological Evolution Of Prion Strains As Amentioning

confidence: 79%

Rodent models for prion diseases

Groschup

Buschmann

2008

Vet. Res.

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-Until today most prion strains can only be propagated and the infectivity content assayed by experimentally challenging conventional or transgenic animals. Robust cell culture systems are not available for any of the natural and only for a few of the experimental prion strains. Moreover, the pathogenesis of different transmissible spongiform encephalopathies (TSE) can be analysed systematically by using experimentally infected animals. While, in the beginning, animals belonging to the natural host species were used, more and more rodent model species have been established, mostly due to practical reasons. Nowadays, most of these experiments are performed using highly susceptible transgenic mouse lines expressing cellular prion proteins, PrP, from a variety of species like cattle, sheep, goat, cervidae, elk, hamster, mouse, mink, pig, and man. In addition, transgenic mice carrying specific mutations or polymorphisms have helped to understand the molecular pathomechanisms of prion diseases. Transgenic mouse models have been utilised to investigate the physiological role of PrP C , molecular aspects of species barrier effects, the cell specificity of the prion propagation, the role of the PrP glycosylation, the mechanisms of the prion spread, the neuropathological roles of PrP C and of its abnormal isoform PrP D (D for disease) as well as the function of PrP Doppel. Transgenic mouse models have also been used for mapping of PrP regions involved in or required for the PrP conversion and prion replication as well as for modelling of familial forms of human prion diseases.

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Prions

Béringue

2015

Reviews in Cell Biology and Molecular Medicine

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Conversion of the BASE Prion Strain into the BSE Strain: The Origin of BSE?

Cited by 151 publications

References 36 publications

Prion agent diversity and species barrier

Prion agent diversity and species barrier

Rodent models for prion diseases

Prions

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