A novel and rapid method for obtaining high titre intact prion strains from mammalian brain
Mammalian prions exist as multiple strains which produce characteristic and highly reproducible phenotypes in defined hosts. How this strain diversity is encoded by a protein-only agent remains one of the most interesting and challenging questions in biology with wide relevance to understanding othe...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Group Publishing
2015
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| Subjects: | |
| Online Access: | https://repository.londonmet.ac.uk/3843/1/srep10062.pdf |
| _version_ | 1804072195288203264 |
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| author | Wenborn, Adam Terry, Cassandra Gros, Nathalie Joiner, Susan D’Castro, Laura Panico, Silvia Sells, Jessica Cronier, Sabrina Linehan, Jacqueline M. Brandner, Sebastian Saibil, Helen R. Collinge, John Wadsworth, Jonathan D. F. |
| author_facet | Wenborn, Adam Terry, Cassandra Gros, Nathalie Joiner, Susan D’Castro, Laura Panico, Silvia Sells, Jessica Cronier, Sabrina Linehan, Jacqueline M. Brandner, Sebastian Saibil, Helen R. Collinge, John Wadsworth, Jonathan D. F. |
| author_sort | Wenborn, Adam |
| collection | LMU |
| description | Mammalian prions exist as multiple strains which produce characteristic and highly reproducible phenotypes in defined hosts. How this strain diversity is encoded by a protein-only agent remains one of the most interesting and challenging questions in biology with wide relevance to understanding other diseases involving the aggregation or polymerisation of misfolded host proteins. Progress in understanding mammalian prion strains has however been severely limited by the complexity and variability of the methods used for their isolation from infected tissue and no high resolution structures have yet been reported. Using high-throughput cell-based prion bioassay to re-examine prion purification from first principles we now report the isolation of prion strains to exceptional levels of purity from small quantities of infected brain and demonstrate faithful retention of biological and biochemical strain properties. The method's effectiveness and simplicity should facilitate its wide application and expedite structural studies of prions. |
| first_indexed | 2024-07-09T03:55:17Z |
| format | Article |
| id | oai:repository.londonmet.ac.uk:3843 |
| institution | London Metropolitan University |
| language | English |
| last_indexed | 2024-07-09T03:55:17Z |
| publishDate | 2015 |
| publisher | Nature Group Publishing |
| record_format | eprints |
| spelling | oai:repository.londonmet.ac.uk:38432020-04-28T14:47:56Z http://repository.londonmet.ac.uk/3843/ A novel and rapid method for obtaining high titre intact prion strains from mammalian brain Wenborn, Adam Terry, Cassandra Gros, Nathalie Joiner, Susan D’Castro, Laura Panico, Silvia Sells, Jessica Cronier, Sabrina Linehan, Jacqueline M. Brandner, Sebastian Saibil, Helen R. Collinge, John Wadsworth, Jonathan D. F. 570 Life sciences; biology Mammalian prions exist as multiple strains which produce characteristic and highly reproducible phenotypes in defined hosts. How this strain diversity is encoded by a protein-only agent remains one of the most interesting and challenging questions in biology with wide relevance to understanding other diseases involving the aggregation or polymerisation of misfolded host proteins. Progress in understanding mammalian prion strains has however been severely limited by the complexity and variability of the methods used for their isolation from infected tissue and no high resolution structures have yet been reported. Using high-throughput cell-based prion bioassay to re-examine prion purification from first principles we now report the isolation of prion strains to exceptional levels of purity from small quantities of infected brain and demonstrate faithful retention of biological and biochemical strain properties. The method's effectiveness and simplicity should facilitate its wide application and expedite structural studies of prions. Nature Group Publishing 2015-05-07 Article PeerReviewed text en https://repository.londonmet.ac.uk/3843/1/srep10062.pdf Wenborn, Adam, Terry, Cassandra, Gros, Nathalie, Joiner, Susan, D’Castro, Laura, Panico, Silvia, Sells, Jessica, Cronier, Sabrina, Linehan, Jacqueline M., Brandner, Sebastian, Saibil, Helen R., Collinge, John and Wadsworth, Jonathan D. F. (2015) A novel and rapid method for obtaining high titre intact prion strains from mammalian brain. Scientific Reports, 5 (1). ISSN 2045-2322 http://dx.doi.org/10.1038/srep10062 10.1038/srep10062 |
| spellingShingle | 570 Life sciences; biology Wenborn, Adam Terry, Cassandra Gros, Nathalie Joiner, Susan D’Castro, Laura Panico, Silvia Sells, Jessica Cronier, Sabrina Linehan, Jacqueline M. Brandner, Sebastian Saibil, Helen R. Collinge, John Wadsworth, Jonathan D. F. A novel and rapid method for obtaining high titre intact prion strains from mammalian brain |
| title | A novel and rapid method for obtaining high titre intact prion strains from mammalian brain |
| title_full | A novel and rapid method for obtaining high titre intact prion strains from mammalian brain |
| title_fullStr | A novel and rapid method for obtaining high titre intact prion strains from mammalian brain |
| title_full_unstemmed | A novel and rapid method for obtaining high titre intact prion strains from mammalian brain |
| title_short | A novel and rapid method for obtaining high titre intact prion strains from mammalian brain |
| title_sort | novel and rapid method for obtaining high titre intact prion strains from mammalian brain |
| topic | 570 Life sciences; biology |
| url | https://repository.londonmet.ac.uk/3843/1/srep10062.pdf |
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