Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their Role
Prion proteins were initially associated with diseases such as Creutzfeldt Jakob and transmissible spongiform encephalopathies. However, deeper research revealed them as versatile tools, exploited by the cells to execute fascinating functions, acting as epigenetic elements or building membrane free...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2015-10-01
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| Series: | Frontiers in Microbiology |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01123/full |
| _version_ | 1818927982302986240 |
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| author | Valentin eIglesias Natalia ede Groot Salvador eVentura |
| author_facet | Valentin eIglesias Natalia ede Groot Salvador eVentura |
| author_sort | Valentin eIglesias |
| collection | DOAJ |
| description | Prion proteins were initially associated with diseases such as Creutzfeldt Jakob and transmissible spongiform encephalopathies. However, deeper research revealed them as versatile tools, exploited by the cells to execute fascinating functions, acting as epigenetic elements or building membrane free compartments in eukaryotes. One of the most intriguing properties of prion proteins is their ability to propagate a conformational assembly, even across species. In this context, it has been observed that bacterial amyloids can trigger the formation of protein aggregates by interacting with host proteins. As our life is closely linked to bacteria, either through a parasitic or symbiotic relationship, prion-like proteins produced by bacterial cells might play a role in this association. Bioinformatics is helping us to understand the factors that determine conformational conversion and infectivity in prion-like proteins. We have used PrionScan to detect prion domains in 839 different bacteria proteomes, detecting 2200 putative prions in these organisms. We studied this set of proteins in order to try to understand their functional role and structural properties. Our results suggest that these bacterial polypeptides are associated to peripheral rearrangement, macromolecular assembly, cell adaptability and invasion. Overall, these data could reveal new threats and therapeutic targets associated to infectious diseases. |
| first_indexed | 2024-12-20T03:21:40Z |
| format | Article |
| id | doaj.art-d708ac88c3b14fc4b562d147025fa65b |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-20T03:21:40Z |
| publishDate | 2015-10-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-d708ac88c3b14fc4b562d147025fa65b2022-12-21T19:55:12ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2015-10-01610.3389/fmicb.2015.01123162802Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their RoleValentin eIglesias0Natalia ede Groot1Salvador eVentura2Universitat Autonoma de BarcelonaUniversitat Autonoma de BarcelonaUniversitat Autonoma de BarcelonaPrion proteins were initially associated with diseases such as Creutzfeldt Jakob and transmissible spongiform encephalopathies. However, deeper research revealed them as versatile tools, exploited by the cells to execute fascinating functions, acting as epigenetic elements or building membrane free compartments in eukaryotes. One of the most intriguing properties of prion proteins is their ability to propagate a conformational assembly, even across species. In this context, it has been observed that bacterial amyloids can trigger the formation of protein aggregates by interacting with host proteins. As our life is closely linked to bacteria, either through a parasitic or symbiotic relationship, prion-like proteins produced by bacterial cells might play a role in this association. Bioinformatics is helping us to understand the factors that determine conformational conversion and infectivity in prion-like proteins. We have used PrionScan to detect prion domains in 839 different bacteria proteomes, detecting 2200 putative prions in these organisms. We studied this set of proteins in order to try to understand their functional role and structural properties. Our results suggest that these bacterial polypeptides are associated to peripheral rearrangement, macromolecular assembly, cell adaptability and invasion. Overall, these data could reveal new threats and therapeutic targets associated to infectious diseases.http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01123/fullAmyloidBacteriaprionPathogenesisprotein aggregation |
| spellingShingle | Valentin eIglesias Natalia ede Groot Salvador eVentura Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their Role Frontiers in Microbiology Amyloid Bacteria prion Pathogenesis protein aggregation |
| title | Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their Role |
| title_full | Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their Role |
| title_fullStr | Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their Role |
| title_full_unstemmed | Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their Role |
| title_short | Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their Role |
| title_sort | computational analysis of candidate prion like proteins in bacteria and their role |
| topic | Amyloid Bacteria prion Pathogenesis protein aggregation |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01123/full |
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