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Cell-to-cell propagation of infectious cytosolic protein aggregates

Title data

Hofmann, Julia P. ; Denner, Philip ; Nussbaum-Krammer, Carmen ; Kuhn, Peer-Hendrik ; Suhre, Michael H. ; Scheibel, Thomas ; Lichtenthaler, Stefan F. ; Schätzl, Hermann M. ; Bano, Daniele ; Vorberg, Ina M.:
Cell-to-cell propagation of infectious cytosolic protein aggregates.
In: Proceedings of the National Academy of Sciences of the United States of America. Vol. 110 (9 April 2013) Issue 15 . - pp. 5951-5956.
ISSN 1091-6490
DOI: https://doi.org/10.1073/pnas.1217321110

Official URL: Volltext

Abstract in another language

Prions are self-templating protein conformers that replicate by recruitment and conversion of homotypic proteins into growing protein aggregates. Originally identified as causative agents of transmissible spongiform encephalopathies, increasing evidence now suggests that prion-like phenomena are more common in nature than previously anticipated. In contrast to fungal prions that replicate in the cytoplasm, propagation of mammalian prions derived from the precursor protein PrP is confined to the cell membrane or endocytic vesicles. Here we demonstrate that cytosolic protein aggregates can also behave as infectious entities in mammalian cells. When expressed in the mammalian cytosol, protein aggregates derived from the prion domain NM of yeast translation termination factor Sup35 persistently propagate and invade neighboring cells, thereby inducing a self-perpetuating aggregation state of NM. Cell contact is required for efficient infection. Aggregates can also be induced in primary astrocytes, neurons, and organotypic cultures, demonstrating that this phenomenon is not specific to immortalized cells. Our data have important implications for understanding prion-like phenomena of protein aggregates associated with human diseases and for the growing number of amyloidogenic proteins discovered in mammals.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Faculties > Faculty of Engineering Science > Chair Biomaterials
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Emerging Fields > Food and Health Sciences
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Emerging Fields
Result of work at the UBT: Yes
DDC Subjects: 600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 19 Jun 2015 06:54
Last Modified: 21 Apr 2016 13:44
URI: https://eref.uni-bayreuth.de/id/eprint/15288