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1.
Vet Res ; 55(1): 62, 2024 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-38750594

RESUMO

The first case of CWD in a Norwegian red deer was detected by a routine ELISA test and confirmed by western blotting and immunohistochemistry in the brain stem of the animal. Two different western blotting tests were conducted independently in two different laboratories, showing that the red deer glycoprofile was different from the Norwegian CWD reindeer and CWD moose and from North American CWD. The isolate showed nevertheless features similar to the classical BSE (BSE-C) strain. Furthermore, BSE-C could not be excluded based on the PrPSc immunohistochemistry staining in the brainstem and the absence of detectable PrPSc in the lymphoid tissues. Because of the known ability of BSE-C to cross species barriers as well as its zoonotic potential, the CWD red deer isolate was submitted to the EURL Strain Typing Expert Group (STEG) as a BSE-C suspect for further investigation. In addition, different strain typing in vivo and in vitro strategies aiming at identifying the BSE-C strain in the red deer isolate were performed independently in three research groups and BSE-C was not found in it. These results suggest that the Norwegian CWD red deer case was infected with a previously unknown CWD type and further investigation is needed to determine the characteristics of this potential new CWD strain.


Assuntos
Cervos , Encefalopatia Espongiforme Bovina , Doença de Emaciação Crônica , Animais , Noruega , Western Blotting/veterinária , Ensaio de Imunoadsorção Enzimática/veterinária , Príons/metabolismo , Bovinos , Imuno-Histoquímica/veterinária , Proteínas PrPSc/metabolismo
2.
Nat Commun ; 15(1): 2112, 2024 Mar 08.
Artigo em Inglês | MEDLINE | ID: mdl-38459071

RESUMO

Prion diseases are a group of rapidly progressing neurodegenerative disorders caused by the misfolding of the endogenous prion protein (PrPC) into a pathogenic form (PrPSc). This process, despite being the central event underlying these disorders, remains largely unknown at a molecular level, precluding the prediction of new potential outbreaks or interspecies transmission incidents. In this work, we present a method to generate bona fide recombinant prions de novo, allowing a comprehensive analysis of protein misfolding across a wide range of prion proteins from mammalian species. We study more than 380 different prion proteins from mammals and classify them according to their spontaneous misfolding propensity and their conformational variability. This study aims to address fundamental questions in the prion research field such as defining infectivity determinants, interspecies transmission barriers or the structural influence of specific amino acids and provide invaluable information for future diagnosis and therapy applications.


Assuntos
Doenças Priônicas , Príons , Animais , Príons/metabolismo , Proteínas Priônicas/genética , Doenças Priônicas/genética , Doenças Priônicas/metabolismo , Mamíferos/metabolismo , Dobramento de Proteína
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