tetano
Editor, Senior Moderator
Sci Rep
. 2021 May 12;11(1):10109.
doi: 10.1038/s41598-021-89586-6.
Neurotropic influenza A virus infection causes prion protein misfolding into infectious prions in neuroblastoma cells
Hideyuki Hara[SUP] 1 [/SUP], Junji Chida[SUP] 1 [/SUP], Keiji Uchiyama[SUP] 1 [/SUP], Agriani Dini Pasiana[SUP] 1 [/SUP], Etsuhisa Takahashi[SUP] 2 [/SUP], Hiroshi Kido[SUP] 2 [/SUP], Suehiro Sakaguchi[SUP] 3 [/SUP]
Affiliations
Abstract
Misfolding of the cellular prion protein, PrP[SUP]C[/SUP], into the amyloidogenic isoform, PrP[SUP]Sc[/SUP], which forms infectious protein aggregates, the so-called prions, is a key pathogenic event in prion diseases. No pathogens other than prions have been identified to induce misfolding of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and propagate infectious prions in infected cells. Here, we found that infection with a neurotropic influenza A virus strain (IAV/WSN) caused misfolding of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and generated infectious prions in mouse neuroblastoma cells through a hit-and-run mechanism. The structural and biochemical characteristics of IAV/WSN-induced PrP[SUP]Sc[/SUP] were different from those of RML and 22L laboratory prions-evoked PrP[SUP]Sc[/SUP], and the pathogenicity of IAV/WSN-induced prions were also different from that of RML and 22L prions, suggesting IAV/WSN-specific formation of PrP[SUP]Sc[/SUP] and infectious prions. Our current results may open a new avenue for the role of viral infection in misfolding of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and formation of infectious prions.
. 2021 May 12;11(1):10109.
doi: 10.1038/s41598-021-89586-6.
Neurotropic influenza A virus infection causes prion protein misfolding into infectious prions in neuroblastoma cells
Hideyuki Hara[SUP] 1 [/SUP], Junji Chida[SUP] 1 [/SUP], Keiji Uchiyama[SUP] 1 [/SUP], Agriani Dini Pasiana[SUP] 1 [/SUP], Etsuhisa Takahashi[SUP] 2 [/SUP], Hiroshi Kido[SUP] 2 [/SUP], Suehiro Sakaguchi[SUP] 3 [/SUP]
Affiliations
- PMID: 33980968
- DOI: 10.1038/s41598-021-89586-6
Abstract
Misfolding of the cellular prion protein, PrP[SUP]C[/SUP], into the amyloidogenic isoform, PrP[SUP]Sc[/SUP], which forms infectious protein aggregates, the so-called prions, is a key pathogenic event in prion diseases. No pathogens other than prions have been identified to induce misfolding of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and propagate infectious prions in infected cells. Here, we found that infection with a neurotropic influenza A virus strain (IAV/WSN) caused misfolding of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and generated infectious prions in mouse neuroblastoma cells through a hit-and-run mechanism. The structural and biochemical characteristics of IAV/WSN-induced PrP[SUP]Sc[/SUP] were different from those of RML and 22L laboratory prions-evoked PrP[SUP]Sc[/SUP], and the pathogenicity of IAV/WSN-induced prions were also different from that of RML and 22L prions, suggesting IAV/WSN-specific formation of PrP[SUP]Sc[/SUP] and infectious prions. Our current results may open a new avenue for the role of viral infection in misfolding of PrP[SUP]C[/SUP] into PrP[SUP]Sc[/SUP] and formation of infectious prions.