Spongiform Encephalopathy in a Miniature Zebu

Seuberlich, Torsten; Botteron, Catherine; Wenker, Christian; Café-Marçal, Valeria Anna; Oevermann, Anna; Haase, Bianca; Leeb, Tosso; Heim, Dagmar; Zurbriggen, Andreas

doi:10.3201/eid1212.060750

Cited by 33 publications

(36 citation statements)

References 14 publications

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“…Its PrP res signature is characterized by protease-resistant fragments of an increased size and a different glycopattern as compared to BSE [27]. Cases have been found so far in France [28], Great Britain [192], Germany [42], the Netherlands [100], USA [164], Sweden [77] and Switzerland (in a zebu, [177]). Like L-type, H-type is transmissible to mice transgenic for bovine PrP, thus establishing its infectious nature [20].…”

Section: Diversity Of Tse Strains In Cattlementioning

confidence: 99%

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: Diversity Of Tse Strains In Cattlementioning

confidence: 99%

Prion agent diversity and species barrier

2008

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“…However, since 2003, unusual cases of BSE have been reported in France, Italy, Belgium, Japan, Germany, the United States and Switzerland [1,6,14,17,21,35,37,42]. Those studies were mostly based on unusual molecular features of PrP res like a triple band pattern due to variations in glycosylation and migration positions because of variable, but often strain-type-dependent, cleavage by proteinase K. Two atypical forms of BSE have been defined: H-type (higher position on the gel with respect to classical BSE) and L-type (lower position when compared with classical BSE) [25].…”

Section: Introductionmentioning

confidence: 99%

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

Polak

Zmudzinski

Jacobs³

et al. 2007

Arch Virol

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SummaryThe aim of this study was to analyze molecular features of protease-resistant prion protein (PrP res ) in Western blots of BSE cases diagnosed in Poland with respect to a possible atypical status. Confirmed cases were analyzed by Western blotting with several monoclonal antibodies directed at N-terminal and core epitopes of prion protein (PrP). Most cases showed the classical glycoprofile characterized by the dominance of the di-over the monoglycosylated PrP res band, yielding di-=mono-ratios well above 2 and by reactivity with antibodies having their epitopes in bovine PrP region 110-242 (Ctype cases). Surprisingly, seven cases of BSE were atypical. Six were classified as L-type based on a slightly lower molecular mass (M r ) of the nonglycosylated band with respect to C-types and a conspicuously low di-=mono-ratio of glycosylated PrP res bands approaching unity. One case was classified as H-type because of a higher M r of PrP res bands on the blot when compared with C-type cases. A characteristic epitope of H-type PrP res occurred in the 101-110 region of PrP for which only antibody 12B2 had a sufficient affinity. The occurrence of atypical cases only in animals 9 years of age and older raises questions about the mechanisms of prion diseases and the origin of BSE.

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“…Another H-type case has been found in a 19 year old miniature zebu in a zoological park in Switzerland [56]. It is noteworthy that atypical cases have been found in countries that did not experience classical BSE so far, like Sweden, or in which only few cases of classical BSE have been found, like Canada or the USA.…”

Section: Atypical Bses and Their Epidemiological Meaningmentioning

confidence: 97%

Review on the epidemiology and dynamics of BSE epidemics

Ducrot¹,

et al. 2008

Self Cite

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-The paper describes how the comprehensive surveillance of bovine spongiform encephalopathy (BSE) and studies carried out on these data has enhanced our knowledge of the epidemiology of BSE. Around 7 000 BSE cases were detected through the screening of about 50 million cattle with rapid tests in Europe. It confirmed that the clinical surveillance had a poor capacity to detect cases, and also showed the discrepancy of this passive surveillance efficiency between regions and production types (dairy/beef). Other risk factors for BSE were being in a dairy herd (three times more than beef), having a young age at first calving (for dairy cattle), being autumn-born (dairy and beef), and being in a herd with a very high milk yield. These findings focus the risk on the feeding regimen of calves/heifers. Several epidemiological studies across countries suggest that the feedborne source related to meat and bone meal (MBM) is the only substantiated route of infection -even after the feed ban -, while it is not possible to exclude maternal transmission or milk replacers as a source of some infections. In most European countries, the average age of the cases is increasing over time and the prevalence decreasing, which reflects the effectiveness of control measures. Consistent results on the trend of the epidemic were obtained using back-calculation modelling, the R 0 approach and Age-Period-Cohort models. Furthermore, active surveillance also resulted in the finding of atypical cases. These are distinct from previously found BSE and classified in two different forms based on biochemical characteristics; their prevalence is very low (36 cases up to 1st September 2007), affected animals were old and some of them displayed clinical signs. The origin and possibility of natural transmission is unknown.

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Spongiform Encephalopathy in a Miniature Zebu

Cited by 33 publications

References 14 publications

Prion agent diversity and species barrier

Prion agent diversity and species barrier

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

Review on the epidemiology and dynamics of BSE epidemics

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