Identification and Characterization of two Bovine Spongiform Encephalopathy cases Diagnosed in the United States

Richt, Jürgen A.; Kunkle, Robert A.; Alt, David P.; Nicholson, E. M.; Hamir, Amir N.; Czub, Stefanie; Kluge, J D; Davis, Al; Hall, Susan

doi:10.1177/104063870701900202

Cited by 96 publications

(113 citation statements)

References 52 publications

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“…Recently, 2 BSE cases identified in cattle born in the United States had unusual PrP res properties similar to those described for H-type BSE ( 11 , 12 , 35 , 36 ), which raised the possibility that atypical TSEs in cattle may be a source for TME infection. In Europe, the prevalence of the H-type or L-type BSE is estimated to be very low (in France the L-type BSE occurs at a prevalence of 1 case found PrP res positive in the brain stem per 3 million cattle tested per year) ( 23 ).…”

Section: Discussionmentioning

confidence: 94%

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

Baron

Bencsik

Biacabe

et al. 2007

Emerg. Infect. Dis.

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Section: Discussionmentioning

confidence: 94%

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

Baron

Bencsik

Biacabe

et al. 2007

Emerg. Infect. Dis.

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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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“…BSE has been transmitted to humans through the consumption of contaminated beef, resulting in the emergence of a new human prion disease, named variant CJD (vCJD), affecting predominantly young adults [31]. Following the occurrence of BSE in three continents since 1986 [32][33][34] the need to ensure the TSE safety of vaccines has become vital. One approach is to avoid, whenever possible, tissues from animals, risk tissues and tissues of unknown or uncertain provenance [35].…”

Section: Page | 24mentioning

confidence: 99%