Publications by authors named "P H Sibille"

Prion diseases, or transmissible spongiform encephalopathies (TSEs), are neurodegenerative disorders caused by the accumulation of misfolded conformers (PrP) of the cellular prion protein (PrP). During the pathogenesis, the PrP seeds disseminate in the central nervous system and convert PrP leading to the formation of insoluble assemblies. As for conventional infectious diseases, variations in the clinical manifestation define a specific prion strain which correspond to different PrP structures.

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Article Synopsis
  • Mammalian prions are infectious proteins formed from misfolded variants of the normal prion protein (PrP), exhibiting different conformations that can self-propagate and cause various prion diseases.
  • Research demonstrates that fibrillar assemblies from recombinant PrP (rPrP) derived from various species (hamster, mouse, human, and bovine) show distinct pathogenic behaviors and strain properties when tested in transgenic mice.
  • The findings indicate that rPrP assemblies can be used to study the transmission of prions and their strain diversity, as they can mimic the adaptation processes of genuine prions despite lacking certain crucial amino acid regions for infectivity.
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Human RSV is the leading cause of infantile bronchiolitis in the world and one of the major causes of childhood deaths in resource-poor settings. It is a major unmet target for vaccines and anti-viral drugs. Respiratory syncytial virus has evolved a unique strategy to evade host immune response by coding for two non-structural proteins NS1 and NS2.

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The purpose of this article is to study the content of a 19th century white porcelain pot from the Pochet-Desroche fabric, offered to the National Order of Pharmacists and probably containing theriac. The aim is to identify the active ingredients of any substances that may still be present and to try to determine the preparation period of the panacea. All the analyzes were carried out according to the reference current methods.

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In peripherally acquired prion diseases, prions move through several tissues of the infected host, notably in the lymphoid tissue, long before the occurrence of neuroinvasion. Accumulation can even be restricted to the lymphoid tissue without neuroinvasion and clinical disease. Several experimental observations indicated that the presence of differentiated follicular dendritic cells (FDCs) in the lymphoid structures and the strain type are critical determinants of prion extraneural replication.

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