tetano
Editor, Senior Moderator
Prion
. 2022 Dec;16(1):1-6.
doi: 10.1080/19336896.2021.2015224.
The first non-prion pathogen identified: neurotropic influenza virus
Suehiro Sakaguchi[SUP] 1 [/SUP], Hideyuki Hara[SUP] 1 [/SUP]
Affiliations
Abstract
The cellular isoform of prion protein, designated PrP[SUP]C[/SUP], is a membrane glycoprotein expressed most abundantly in the brain, particularly by neurons, and its conformational conversion into the abnormally folded, amyloidogenic isoform, PrP[SUP]Sc[/SUP], is an underlying mechanism in the pathogenesis of prion diseases, a group of neurodegenerative disorders in humans and animals. Most cases of these diseases are sporadic and their aetiologies are unknown. We recently found that a neurotropic strain of influenza A virus (IAV/WSN) caused the conversion of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and the subsequent formation of infectious prions in mouse neuroblastoma cells after infection. These results show that IAV/WSN is the first non-prion pathogen capable of inducing the conversion of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and propagating infectious prions in cultured neuronal cells, and also provide the intriguing possibility that IAV infection in neurons might be a cause of or be associated with sporadic prion diseases. Here, we present our findings of the IAV/WSN-induced conversion of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and subsequent propagation of infectious prions, and also discuss the biological significance of the conversion of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] in virus infections.
Keywords: Prion; conformational conversion; influenza virus; neurodegenerative disease; prion disease; prion protein; protein polymerization; virus infection.
. 2022 Dec;16(1):1-6.
doi: 10.1080/19336896.2021.2015224.
The first non-prion pathogen identified: neurotropic influenza virus
Suehiro Sakaguchi[SUP] 1 [/SUP], Hideyuki Hara[SUP] 1 [/SUP]
Affiliations
- PMID: 34978525
- DOI: 10.1080/19336896.2021.2015224
Abstract
The cellular isoform of prion protein, designated PrP[SUP]C[/SUP], is a membrane glycoprotein expressed most abundantly in the brain, particularly by neurons, and its conformational conversion into the abnormally folded, amyloidogenic isoform, PrP[SUP]Sc[/SUP], is an underlying mechanism in the pathogenesis of prion diseases, a group of neurodegenerative disorders in humans and animals. Most cases of these diseases are sporadic and their aetiologies are unknown. We recently found that a neurotropic strain of influenza A virus (IAV/WSN) caused the conversion of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and the subsequent formation of infectious prions in mouse neuroblastoma cells after infection. These results show that IAV/WSN is the first non-prion pathogen capable of inducing the conversion of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and propagating infectious prions in cultured neuronal cells, and also provide the intriguing possibility that IAV infection in neurons might be a cause of or be associated with sporadic prion diseases. Here, we present our findings of the IAV/WSN-induced conversion of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and subsequent propagation of infectious prions, and also discuss the biological significance of the conversion of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] in virus infections.
Keywords: Prion; conformational conversion; influenza virus; neurodegenerative disease; prion disease; prion protein; protein polymerization; virus infection.