Grass Plants Bind, Retain, Uptake, and Transport Infectious Prions
Pritzkow, Sandra et al.
Cell Reports , Volume 11 , Issue 8 , 1168 - 1175 Highlights
Summary
Prions are the protein-based infectious agents responsible for prion diseases. Environmental prion contamination has been implicated in disease transmission. Here, we analyzed the binding and retention of infectious prion protein (PrPSc) to plants. Small quantities of PrPSc contained in diluted brain homogenate or in excretory materials (urine and feces) can bind to wheat grass roots and leaves. Wild-type hamsters were efficiently infected by ingestion of prion-contaminated plants. The prion-plant interaction occurs with prions from diverse origins, including chronic wasting disease. Furthermore, leaves contaminated by spraying with a prion-containing preparation retained PrPSc for several weeks in the living plant. Finally, plants can uptake prions from contaminated soil and transport them to aerial parts of the plant (stem and leaves). These findings demonstrate that plants can efficiently bind infectious prions and act as carriers of infectivity, suggesting a possible role of environmental prion contamination in the horizontal transmission of the disease.
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Received: October 31, 2014; Received in revised form: February 4, 2015; Accepted: April 15, 2015; Published Online: May 14, 2015
? 2015 The Authors. Published by Elsevier Inc.
Pritzkow, Sandra et al.
Cell Reports , Volume 11 , Issue 8 , 1168 - 1175 Highlights
- ?Grass plants bind prions from contaminated brain and excreta
- ?Prions from different strains and species remain bound to living plants
- ?Hamsters fed with prion-contaminated plant samples develop prion disease
- ?Stems and leaves from grass plants grown in infected soil contain prions
Summary
Prions are the protein-based infectious agents responsible for prion diseases. Environmental prion contamination has been implicated in disease transmission. Here, we analyzed the binding and retention of infectious prion protein (PrPSc) to plants. Small quantities of PrPSc contained in diluted brain homogenate or in excretory materials (urine and feces) can bind to wheat grass roots and leaves. Wild-type hamsters were efficiently infected by ingestion of prion-contaminated plants. The prion-plant interaction occurs with prions from diverse origins, including chronic wasting disease. Furthermore, leaves contaminated by spraying with a prion-containing preparation retained PrPSc for several weeks in the living plant. Finally, plants can uptake prions from contaminated soil and transport them to aerial parts of the plant (stem and leaves). These findings demonstrate that plants can efficiently bind infectious prions and act as carriers of infectivity, suggesting a possible role of environmental prion contamination in the horizontal transmission of the disease.
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Received: October 31, 2014; Received in revised form: February 4, 2015; Accepted: April 15, 2015; Published Online: May 14, 2015
? 2015 The Authors. Published by Elsevier Inc.
Full text
Comment