The mechanism of monomer transfer between two structurally distinct PrP oligomers
In mammals, Prion pathology refers to a class of infectious neuropathologies whose mechanism is based on the self-perpetuation of structural information stored in the pathological conformer. The characterisation of the PrP folding landscape has revealed the existence of a plethora of pathways conduc...
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| Veröffentlicht in: | PloS one 2017-07, Vol.12 (7), p.e0180538 |
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| creator | Armiento, Aurora Moireau, Philippe Martin, Davy Lepejova, Nad'a Doumic, Marie Rezaei, Human |
| description | In mammals, Prion pathology refers to a class of infectious neuropathologies whose mechanism is based on the self-perpetuation of structural information stored in the pathological conformer. The characterisation of the PrP folding landscape has revealed the existence of a plethora of pathways conducing to the formation of structurally different assemblies with different biological properties. However, the biochemical interconnection between these diverse assemblies remains unclear. The PrP oligomerisation process leads to the formation of neurotoxic and soluble assemblies called O1 oligomers with a high size heterodispersity. By combining the measurements in time of size distribution and average size with kinetic models and data assimilation, we revealed the existence of at least two structurally distinct sets of assemblies, termed Oa and Ob, forming O1 assemblies. We propose a kinetic model representing the main processes in prion aggregation pathway: polymerisation, depolymerisation, and disintegration. The two groups interact by exchanging monomers through a disintegration process that increases the size of Oa. Our observations suggest that PrP oligomers constitute a highly dynamic population. |
| doi_str_mv | 10.1371/journal.pone.0180538 |
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The characterisation of the PrP folding landscape has revealed the existence of a plethora of pathways conducing to the formation of structurally different assemblies with different biological properties. However, the biochemical interconnection between these diverse assemblies remains unclear. The PrP oligomerisation process leads to the formation of neurotoxic and soluble assemblies called O1 oligomers with a high size heterodispersity. By combining the measurements in time of size distribution and average size with kinetic models and data assimilation, we revealed the existence of at least two structurally distinct sets of assemblies, termed Oa and Ob, forming O1 assemblies. We propose a kinetic model representing the main processes in prion aggregation pathway: polymerisation, depolymerisation, and disintegration. The two groups interact by exchanging monomers through a disintegration process that increases the size of Oa. 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The characterisation of the PrP folding landscape has revealed the existence of a plethora of pathways conducing to the formation of structurally different assemblies with different biological properties. However, the biochemical interconnection between these diverse assemblies remains unclear. The PrP oligomerisation process leads to the formation of neurotoxic and soluble assemblies called O1 oligomers with a high size heterodispersity. By combining the measurements in time of size distribution and average size with kinetic models and data assimilation, we revealed the existence of at least two structurally distinct sets of assemblies, termed Oa and Ob, forming O1 assemblies. We propose a kinetic model representing the main processes in prion aggregation pathway: polymerisation, depolymerisation, and disintegration. The two groups interact by exchanging monomers through a disintegration process that increases the size of Oa. 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The characterisation of the PrP folding landscape has revealed the existence of a plethora of pathways conducing to the formation of structurally different assemblies with different biological properties. However, the biochemical interconnection between these diverse assemblies remains unclear. The PrP oligomerisation process leads to the formation of neurotoxic and soluble assemblies called O1 oligomers with a high size heterodispersity. By combining the measurements in time of size distribution and average size with kinetic models and data assimilation, we revealed the existence of at least two structurally distinct sets of assemblies, termed Oa and Ob, forming O1 assemblies. We propose a kinetic model representing the main processes in prion aggregation pathway: polymerisation, depolymerisation, and disintegration. The two groups interact by exchanging monomers through a disintegration process that increases the size of Oa. Our observations suggest that PrP oligomers constitute a highly dynamic population.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>28746342</pmid><doi>10.1371/journal.pone.0180538</doi><tpages>e0180538</tpages><orcidid>https://orcid.org/0000-0002-3183-8215</orcidid><orcidid>https://orcid.org/0000-0003-2421-716X</orcidid><orcidid>https://orcid.org/0000-0001-9996-5213</orcidid><orcidid>https://orcid.org/0000-0001-9672-748X</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Agglomeration Algorithms Analysis Analysis of PDEs Animals Applied mathematics Assemblies Biochemistry, Molecular Biology Biological properties Chromatography Computer Simulation Creutzfeldt-Jakob disease Data assimilation Data collection Disintegration Kinetics Life Sciences Mathematics Medicine and Health Sciences Models, Chemical Molecular biology Molecular weight Monomers Neurotoxicity Oligomers Physical Sciences Polymerization Prions Prions - chemistry Protein Aggregates Protein Aggregation, Pathological Protein Multimerization Protein Unfolding Proteins Research and Analysis Methods Sheep Size distribution |
| title | The mechanism of monomer transfer between two structurally distinct PrP oligomers |
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