The mechanisms of humic substances self-assembly with biological molecules: The case study of the prion protein.
Humic substances (HS) are the largest constituent of soil organic matter and are considered as a key component of the terrestrial ecosystem. HS may facilitate the transport of organic and inorganic molecules, as well as the sorption interactions with environmentally relevant proteins such as prions....
Main Authors: | , , , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2017-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC5697873?pdf=render |
id |
doaj-1126c4d3fc2544c1810bfb4695ab5fa5 |
---|---|
record_format |
Article |
spelling |
doaj-1126c4d3fc2544c1810bfb4695ab5fa52020-11-25T01:46:37ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-011211e018830810.1371/journal.pone.0188308The mechanisms of humic substances self-assembly with biological molecules: The case study of the prion protein.Gabriele GiachinRidvan NepravishtaWalter MandalitiSonia MelinoAlja MargonDenis ScainiPierluigi MazzeiAlessandro PiccoloGiuseppe LegnameMaurizio PaciLiviana LeitaHumic substances (HS) are the largest constituent of soil organic matter and are considered as a key component of the terrestrial ecosystem. HS may facilitate the transport of organic and inorganic molecules, as well as the sorption interactions with environmentally relevant proteins such as prions. Prions enter the environment through shedding from live hosts, facilitating a sustained incidence of animal prion diseases such as Chronic Wasting Disease and scrapie in cervid and ovine populations, respectively. Changes in prion structure upon environmental exposure may be significant as they can affect prion infectivity and disease pathology. Despite its relevance, the mechanisms of prion interaction with HS are still not completely understood. The goal of this work is to advance a structural-level picture of the encapsulation of recombinant, non-infectious, prion protein (PrP) into different natural HS. We observed that PrP precipitation upon addition of HS is mainly driven by a mechanism of "salting-out" whereby PrP molecules are rapidly removed from the solution and aggregate in insoluble adducts with humic molecules. Importantly, this process does not alter the protein folding since insoluble PrP retains its α-helical content when in complex with HS. The observed ability of HS to promote PrP insolubilization without altering its secondary structure may have potential relevance in the context of "prion ecology". These results suggest that soil organic matter interacts with prions possibly without altering the protein structures. This may facilitate prions preservation from biotic and abiotic degradation leading to their accumulation in the environment.http://europepmc.org/articles/PMC5697873?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Gabriele Giachin Ridvan Nepravishta Walter Mandaliti Sonia Melino Alja Margon Denis Scaini Pierluigi Mazzei Alessandro Piccolo Giuseppe Legname Maurizio Paci Liviana Leita |
spellingShingle |
Gabriele Giachin Ridvan Nepravishta Walter Mandaliti Sonia Melino Alja Margon Denis Scaini Pierluigi Mazzei Alessandro Piccolo Giuseppe Legname Maurizio Paci Liviana Leita The mechanisms of humic substances self-assembly with biological molecules: The case study of the prion protein. PLoS ONE |
author_facet |
Gabriele Giachin Ridvan Nepravishta Walter Mandaliti Sonia Melino Alja Margon Denis Scaini Pierluigi Mazzei Alessandro Piccolo Giuseppe Legname Maurizio Paci Liviana Leita |
author_sort |
Gabriele Giachin |
title |
The mechanisms of humic substances self-assembly with biological molecules: The case study of the prion protein. |
title_short |
The mechanisms of humic substances self-assembly with biological molecules: The case study of the prion protein. |
title_full |
The mechanisms of humic substances self-assembly with biological molecules: The case study of the prion protein. |
title_fullStr |
The mechanisms of humic substances self-assembly with biological molecules: The case study of the prion protein. |
title_full_unstemmed |
The mechanisms of humic substances self-assembly with biological molecules: The case study of the prion protein. |
title_sort |
mechanisms of humic substances self-assembly with biological molecules: the case study of the prion protein. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2017-01-01 |
description |
Humic substances (HS) are the largest constituent of soil organic matter and are considered as a key component of the terrestrial ecosystem. HS may facilitate the transport of organic and inorganic molecules, as well as the sorption interactions with environmentally relevant proteins such as prions. Prions enter the environment through shedding from live hosts, facilitating a sustained incidence of animal prion diseases such as Chronic Wasting Disease and scrapie in cervid and ovine populations, respectively. Changes in prion structure upon environmental exposure may be significant as they can affect prion infectivity and disease pathology. Despite its relevance, the mechanisms of prion interaction with HS are still not completely understood. The goal of this work is to advance a structural-level picture of the encapsulation of recombinant, non-infectious, prion protein (PrP) into different natural HS. We observed that PrP precipitation upon addition of HS is mainly driven by a mechanism of "salting-out" whereby PrP molecules are rapidly removed from the solution and aggregate in insoluble adducts with humic molecules. Importantly, this process does not alter the protein folding since insoluble PrP retains its α-helical content when in complex with HS. The observed ability of HS to promote PrP insolubilization without altering its secondary structure may have potential relevance in the context of "prion ecology". These results suggest that soil organic matter interacts with prions possibly without altering the protein structures. This may facilitate prions preservation from biotic and abiotic degradation leading to their accumulation in the environment. |
url |
http://europepmc.org/articles/PMC5697873?pdf=render |
work_keys_str_mv |
AT gabrielegiachin themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT ridvannepravishta themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT waltermandaliti themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT soniamelino themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT aljamargon themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT denisscaini themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT pierluigimazzei themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT alessandropiccolo themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT giuseppelegname themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT mauriziopaci themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT livianaleita themechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT gabrielegiachin mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT ridvannepravishta mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT waltermandaliti mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT soniamelino mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT aljamargon mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT denisscaini mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT pierluigimazzei mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT alessandropiccolo mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT giuseppelegname mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT mauriziopaci mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein AT livianaleita mechanismsofhumicsubstancesselfassemblywithbiologicalmoleculesthecasestudyoftheprionprotein |
_version_ |
1725018278246481920 |