Logo des Robert Koch-InstitutLogo des Robert Koch-Institut
Publikationsserver des Robert Koch-Institutsedoc
de|en
Publikation anzeigen 
  • edoc Startseite
  • Artikel in Fachzeitschriften
  • Artikel in Fachzeitschriften
  • Publikation anzeigen
  • edoc Startseite
  • Artikel in Fachzeitschriften
  • Artikel in Fachzeitschriften
  • Publikation anzeigen
JavaScript is disabled for your browser. Some features of this site may not work without it.
Gesamter edoc-ServerBereiche & SammlungenTitelAutorSchlagwortDiese SammlungTitelAutorSchlagwort
PublizierenEinloggenRegistrierenHilfe
StatistikNutzungsstatistik
Gesamter edoc-ServerBereiche & SammlungenTitelAutorSchlagwortDiese SammlungTitelAutorSchlagwort
PublizierenEinloggenRegistrierenHilfe
StatistikNutzungsstatistik
Publikation anzeigen 
  • edoc Startseite
  • Artikel in Fachzeitschriften
  • Artikel in Fachzeitschriften
  • Publikation anzeigen
  • edoc Startseite
  • Artikel in Fachzeitschriften
  • Artikel in Fachzeitschriften
  • Publikation anzeigen
2016-09-09Zeitschriftenartikel DOI: 10.1038/srep33119
Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation
Katorcha, Elizaveta
Daus, Martin L.
Gonzalez-Montalban, Nuria
Makarava, Natallia
Lasch, Peter
Beekes, Michael
Baskakov, Ilia V.
The innate immune system provides the first line of defense against pathogens. To recognize pathogens, this system detects a number of molecular features that discriminate pathogens from host cells, including terminal sialylation of cell surface glycans. Mammalian cell surfaces, but generally not microbial cell surfaces, have sialylated glycans. Prions or PrPSc are proteinaceous pathogens that lack coding nucleic acids but do possess sialylated glycans. We proposed that sialylation of PrPSc is essential for evading innate immunity and infecting a host. In this study, the sialylation status of PrPSc was reduced by replicating PrPSc in serial Protein Misfolding Cyclic Amplification using sialidase-treated PrPC substrate and then restored to original levels by replication using non-treated substrate. Upon intracerebral administration, all animals that received PrPSc with original or restored sialylation levels were infected, whereas none of the animals that received PrPSc with reduced sialylation were infected. Moreover, brains and spleens of animals from the latter group were completely cleared of prions. The current work established that the ability of prions to infect the host via intracerebral administration depends on PrPSc sialylation status. Remarkably, PrPSc infectivity could be switched off and on in a reversible manner by first removing and then restoring PrPSc sialylation.
Dateien zu dieser Publikation
Thumbnail
226tXlwolqBWc.pdf — PDF — 844.3 Kb
MD5: b1b94d77a1c7d95da686f1cdfff02185
Zitieren
BibTeX
EndNote
RIS
Keine Lizenzangabe
Zur Langanzeige
Nutzungsbedingungen Impressum Leitlinien Datenschutzerklärung Kontakt

Das Robert Koch-Institut ist ein Bundesinstitut im

Geschäftsbereich des Bundesministeriums für Gesundheit

© Robert Koch Institut

Alle Rechte vorbehalten, soweit nicht ausdrücklich anders vermerkt.

 
DOI
10.1038/srep33119
Permanent URL
https://doi.org/10.1038/srep33119
HTML
<a href="https://doi.org/10.1038/srep33119">https://doi.org/10.1038/srep33119</a>