Atypical status of bovine spongiform encephalopathy in Poland: a molecular typing study

Polak, M.P.; Zmudzinski, J.F.; Jacobs, J.G.; Langeveld, J.P.M.

doi:10.1007/s00705-007-1062-6

Cited by 42 publications

(39 citation statements)

References 38 publications

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“…Recently, L-type BSE cases were detected in several countries, 13,14,16,18,19 and their characteristics were investigated. 16,20,30,31 It has been reported that the European L-type BSE has a distinct glycoform of PrP Sc that has relatively weaker PK resistance.…”

Section: Discussionmentioning

confidence: 99%

“…[8][9][10][11][12] In recent years, several cases of atypical neuropathological and molecular phenotypes of BSE (atypical BSE) have been reported in Japan, several European countries and North America. [13][14][15][16][17][18][19] Atypical BSE cases are temporally classified into two groups-L-type and H-type-according to the molecular size of the proteinase K (PK) digested non-glycosylated form of PrP Sc . 18 However, the precise definition of atypical BSE prions remains to be established.…”

Section: Introductionmentioning

confidence: 99%

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Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle

Masujin

Shu

Yamakawa

et al. 2008

Prion

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A case of L-type-like atypical bovine spongiform encephalopathy was detected in 14-year-old Japanese black beef cattle (BSE/ JP24). To clarify the biological and biochemical properties of the prion in BSE/JP24, we performed a transmission study with wildtype mice and bovinized transgenic mice (TgBoPrP). The BSE/ JP24 prion was transmitted to TgBoPrP mice with the incubation period of 199.7 ± 3.4 days, which was shorter than that of classical BSE (C-BSE) (223.5 ± 13.5 days). Further, C-BSE was transmitted to wild-type mice with the incubation period of about 409 days, whereas BSE/JP24 prion inoculated mice showed no clinical signs up to 649 days. Severe vacuolation and a widespread and uniform distribution of PrP Sc were pathologically observed in the brain of BSE/JP24 prion affected TgBoPrP mice. The molecular weight and glycoform ratio of PrP Sc in BSE/JP24 were different from those in C-BSE, and PrP Sc in BSE/JP24 exhibited weaker proteinase K resistance than that in C-BSE. These findings revealed that the BSE/JP24 prion has distinct biological and biochemical properties reported for that of C-BSE. Interestingly, a shorter incubation period was observed at the subsequent passage of the BSE/JP24 prion to TgBoPrP mice (152.2 ± 3.1 days). This result implies that BSE/JP24 prion has newly emerged and showed the possibility that L-type BSE prion might be classified into multiple strains.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle

Masujin

Shu

Yamakawa

et al. 2008

Prion

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“…In addition to the L-type group already mentioned (see Sect. 3.3.2), which has been identified in France [28], Italy [47], Germany [42] and Poland [151], a second group termed H-type has been found. Its PrP res signature is characterized by protease-resistant fragments of an increased size and a different glycopattern as compared to BSE [27].…”

Section: Diversity Of Tse Strains In Cattlementioning

confidence: 92%

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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“…Scientific studies report information on the identification of L-BSE in France , Italy , Germany (Buschmann et al, 2006), Great Britain (Stack et al, 2013) and Poland (Polak et al, 2008). H-BSE has been reported in France , Great Britain (Terry et al, 2007), Germany (Buschmann et al, 2006), the Netherlands (Jacobs et al, 2007) and Sweden (Gavier-Widen et al, 2008).…”

Section: And Data Reported By Member States To the European Commissiomentioning

confidence: 99%

Protocol for further laboratory investigations into the distribution of infectivity of Atypical BSE

2014

EFSA Journal

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Information on the pathogenesis and tissue distribution of Atypical Bovine Spongiform Encephalopathy (BSE) in cattle through the study of field cases and experimental transmission studies is lacking. The latter are limited to transmission of Atypical BSE through intracerebral (i.c.) inoculation of cattle. All data currently available relate to the presence or absence of PrP Sc , but do not quantify relative amounts of PrP Sc or levels of infectivity. A laboratory protocol for further studies is recommended, to allow the assessment of the relative infectious titre, PrP Sc accumulation and prion seeding activity in the tissues of cattle that developed H-BSE or L-BSE (using posterior brainstem as a reference). Tissues to be covered by those studies are categorised in three priorities, based on their inclusion in the list of specific risk material in cattle, on the presence of infectivity, or PrP Sc presence, demonstrated in Atypical BSEs or other Transmissible Spongiform Encephalopathies (TSEs) in ruminants, and on the importance in terms of input into the food chain in the EU. The protocol provides details in terms of the minimum number of animals to be tested, processing and preparation of tissues, and methods to be used to identify abnormal PrP and quantify infectivity, also depending on the expected level of infectivity and amount of tissue available for analysis. It is recommended that, through the implementation of the protocol, information should also be obtained on the performance of currently validated rapid tests for TSE active surveillance in cattle/bioassay for detecting H-BSE and L-BSE agents.

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Atypical status of bovine spongiform encephalopathy in Poland: a molecular typing study

Cited by 42 publications

References 38 publications

Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle

Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle

Prion agent diversity and species barrier

Protocol for further laboratory investigations into the distribution of infectivity of Atypical BSE

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