BACKGROUND Sporadic Creutzfeldt-Jakob disease (sCJD) is a rare neurodegenerative disorder in humans included in the group of Transmissible Spongiform Encephalopathies or prion diseases. The vast majority of sCJD cases are molecularly classified according to the abnormal prion protein (PrPSc) conformations along with polymorphism of codon 129 of the PRNP gene. Recently, a novel human disease, te...

Prion diseases are fatal transmissible neurodegenerative disorders of both animals and humans associated with prolonged incubation periods and include scrapie, bovine spongiform encephalopathy (BSE) and Creutzfeldt-Jakob disease (CJD). The arrival of variant CJD (vCJD) and the recognition that it is causally related to BSE, to which there has been widespread dietary exposure, has lead to consid...

Prion diseases are fatal neurodegenerative disorders caused by accumulation of abnormal prion protein (protease-resistant prion, PrPres). PrPres accumulation is also detected in lymphoid organs after peripheral infection. Several studies suggest that follicular dendritic cells (FDC) could be the site of PrPres retention and amplification. Here we show that human follicular dendritic cells can e...

Using different prion strains, such as the variant Creutzfeldt-Jakob disease agent and the atypical bovine spongiform encephalopathy agents, and using transgenic mice expressing human or bovine prion protein, we assessed the reliability of protein misfolding cyclic amplification (PMCA) to model interspecies and genetic barriers to prion transmission. We compared our PMCA results with in vivo tr...

Prion diseases are widely recognized for their transmissibility, and it is this feature that has been studied most extensively. In recent years, public health concerns over the transmission of animal forms of prion disease, such as bovine spongiform encephalopathy and chronic wasting disease, to humans has only augmented the notion that prion diseases are primarily infectious. Yet within the sp...

A crucial tenet of the prion hypothesis is that misfolding of the prion protein (PrP) induced by mutations associated with familial prion disease is, in an otherwise normal mammalian brain, sufficient to generate the infectious agent. Yet this has never been demonstrated. We engineered knockin mice to express a PrP mutation associated with a distinct human prion disease, fatal familial insomnia...

Prion diseases are fatal brain disorders characterized by deposition of insoluble isoforms the prion protein (PrP). The normal and pathogenic structures PrP relatively well known after decades studies. Yet our current understanding intrinsic determinants regulating misfolding largely missing. A 3D subdomain comprising β2-α2 loop helix 3 contains high sequence structural variability among animal...

If the attacking force has a vaccine before attack, will inflict crippling damage on enemy. Thus, virus emerges as potential danger since they can be used in development of such weapons. The reported neurotropic strain influenza A (IAV) induced conversion normal prion protein (PrPC) into infectious (PrPSc) well formation prions bring out type prion/virus unprecedented pathogens that cause fatal...