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Prions made in the lab

Date:
January 4, 2016
Source:
Sissa Medialab
Summary:
At times, to understand something well, it is useful to rebuild  it from scratch. It happens with prions as well, say researchers who assembled artificial prions, devising a method for synthesizing them in a series. Lab tests showed that synthetic prions act like their biological counterparts.
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At times, to understand something well, it is useful to rebuild it from scratch. It happens with prions as well: in collaboration with the BESTA Institute in Milan, the Laboratory of Prion Biology at SISSA in Trieste assembled artificial prions, devising a method for synthesizing them in a series. Lab tests showed that synthetic prions act like their biological counterparts. Results will be published on December 31 in Plos Pathogens.

"They will help us understand the precise mechanisms by which prions cause illnesses like Mad Cow or Creutzfeldt-Jakob disease." SISSA, in collaboration with the Carlo Besta Neurological Institute in Milan, established ideal lab conditions to create synthetic prions which act like biological ones, in a repetitive manner. "It is the first time that something like this has been done, and the consequences for research are significant."

Synthetic prions produced in a series allow precise control over their pathogenic behavior in experiments," explains Giuseppe Legname, coordinator of the study whose lab techniques and results will be published in Plos Pathogens. Working with "natural" prions is not always so simple. "They are complex and heterogeneous," says Legname, noting they are often complicated to use. "The synthetic ones we created ourselves, however, are easier to control, homogeneous and structurally defined. And yet they still show the same consequences as biological ones. Our ultimate goal, of course, is to identify mechanisms which can block the pathogenic effect, in order to develop treatments for disease."

In the study, Legname and colleagues synthesized mouse prions, verifying their role in causing illness, which proved comparable to natural prions. "When we 'characterized' them, we also observed that they were very similar to the ones responsible for Mad Cow and Creutzfeldt-Jakob disease, the human form of the illness."

Not just "Mad Cow"

"Naturally, our line of research is already evolving. We will be working with human prions, and we have other projects as well," says Legname. He is referring to the hypothesis which is becoming more and more scientifically sound, that at the base of most neurodegenerative disease there are molecules with mechanisms similar to those of prions. "We are thinking about the molecules responsible for Alzheimers, like amyloid beta, or Parkinsons, or even amyotrophic lateral sclerosis. In these cases as well, having synthetic molecules available could be an important step forward."


Story Source:

Materials provided by Sissa Medialab. Note: Content may be edited for style and length.


Journal Reference:

  1. Fabio Moda, Thanh-Nhat T. Le, Suzana Aulić, Edoardo Bistaffa, Ilaria Campagnani, Tommaso Virgilio, Antonio Indaco, Luisa Palamara, Olivier Andréoletti, Fabrizio Tagliavini, Giuseppe Legname. Synthetic prions with novel strain-specified properties. PLOS Pathogens, 2015; 11 (12): e1005354 DOI: 10.1371/journal.ppat.1005354

Cite This Page:

Sissa Medialab. "Prions made in the lab." ScienceDaily. ScienceDaily, 4 January 2016. <www.sciencedaily.com/releases/2016/01/160104081251.htm>.
Sissa Medialab. (2016, January 4). Prions made in the lab. ScienceDaily. Retrieved March 28, 2024 from www.sciencedaily.com/releases/2016/01/160104081251.htm
Sissa Medialab. "Prions made in the lab." ScienceDaily. www.sciencedaily.com/releases/2016/01/160104081251.htm (accessed March 28, 2024).

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