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Press Release - Prion diseases: new clues in the structure of prion proteins

Carbohydrates of the prion glycoproteins responsible for a group of neurodegenerative diseases were sequenced for the first time thanks to a highly sensitive technique. The paper is now published in PLOS Pathogens and represents another step toward the fully understanding of these fatal disorders



        Image: Photomicrograph of a neural tissue specimen, harvested from a scrapie affected 
        mouse, revealing the presence of prion protein stained in red.
        Credits: National Institute of Allergy and Infectious Diseases (NIAID)


18 February 2021
Prion diseases are a group of rapidly progressive, fatal and infectious neurodegenerative disorders affecting both humans and animals: Bovine Spongiform Encephalopathy (BSE) or ‘mad cow’ disease is one of the most famous since in 1996 scientists found that the agent responsible for the disease in cows, is the same agent responsible for the so-called variant Creutzfeldt-Jakob Disease (vCJD), a disease affecting humans.
A new study carried out by SISSA – Scuola Internazionale Superiore di Studi Avanzati in collaboration with other institutions including Genos Glycoscience Research Laboratory from Zagreb, Croatia and Elettra Sincrotrone Trieste, provides important information on the differences in structures of the prions, proteins responsible for diseases that at the state of the art are incurable.

The mystery of the strains

One of the main unanswered problems revolving around prion diseases is the existence of strains, leading to a wide range of disorders with different symptoms, incubation time, histopathology, etc. “For a better understanding of the mechanism of the diseases and the existence of strains, resolving the structure of the prion protein is necessary” neuroscientist Natali Nakić, first author of the paper “Site-specific analysis of N-glycans from different sheep prion strains”, just published in PLOS Pathogens, says.

The prion protein is a glycoprotein, meaning polysaccharides called glycans encompass a large part of the protein structure. The new study is the first one of its kind as it focuses on comparing glycan structures from different strains.

Professor Giuseppe Legname, co-author of the paper, is the Director of SISSA Prion Biology Laboratory and has been collaborating with Elettra Sincrotrone Trieste since 2006: “Carbohydrate of the glycoproteins were sequenced for the first time thanks to the collaboration with Genos Glycoscience Research Laboratory, using a highly sensitive technique called Liquid Chromatography/Mass Spectrometry” he says. “It has long been questioned whether the diversity in prion strains may depend on the glycans that compose them as well as on protein folding. Our results led us to an answer for the first time”.

A step toward the fully understanding

In this study, glycans from two different sheep prion strains were comparedNatali Nakić adds. “After an extensive analysis, no major differences in glycan structures were found between the two strains, suggesting that glycans may not be responsible for the biochemical and neuropathological differences”. A remarkable goal as it represents another step toward the fully understanding of prion glycoproteins and the cellular mechanism of prion diseases.


Press Release:
"Prion diseases: new clues in the structure of prion proteins"  pdf

Original Article:
"Site-specific analysis of N-glycans from different sheep prion strains" pdf

Contacts:
SISSA

Marina D’Alessandro
e-mail: marina.dalessandro@sissa.it
M +39 349 2885935

Elettra Sincrotrone Trieste
Marco Marazzi
e-mail: marco.marazzi@elettra.eu
M + 39 335 6073350

Genos Glycoscience
Marina Martinic Kavur
e-mail: mkavur@genos.hr
M +38 591 6037582
 

Press Review

Triestecafè.it dd 19/02/2021: "Sequenziati a Trieste per la prima volta i carboidrati dei prioni, responsabili di malattie neurodegenerative"



 

 
Last Updated on Friday, 05 March 2021 11:17