[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"detail-sidebar-cat-0-en-105":3,"doc-seo-441855-105":59,"doc-detail-441855-en":129},{"code":4,"msg":5,"data":6},0,"success",[7,13,18,23,28,33,38,43,48,51,55],{"id":8,"doc_module":4,"doc_module_name":9,"category_name":10,"show_sort_weight":11,"slug":12},1,"Document","Story & Novel",90,"story-novel",{"id":14,"doc_module":4,"doc_module_name":9,"category_name":15,"show_sort_weight":16,"slug":17},2,"Literature",80,"literature",{"id":19,"doc_module":4,"doc_module_name":9,"category_name":20,"show_sort_weight":21,"slug":22},4,"Exam",70,"exam",{"id":24,"doc_module":4,"doc_module_name":9,"category_name":25,"show_sort_weight":26,"slug":27},5,"Comic",60,"comic",{"id":29,"doc_module":4,"doc_module_name":9,"category_name":30,"show_sort_weight":31,"slug":32},6,"Technology",50,"technology",{"id":34,"doc_module":4,"doc_module_name":9,"category_name":35,"show_sort_weight":36,"slug":37},7,"Healthcare",40,"healthcare",{"id":39,"doc_module":4,"doc_module_name":9,"category_name":40,"show_sort_weight":41,"slug":42},8,"Research & Report",30,"research-report",{"id":44,"doc_module":4,"doc_module_name":9,"category_name":45,"show_sort_weight":46,"slug":47},9,"Religion & Spirituality",20,"religion-spirituality",{"id":46,"doc_module":4,"doc_module_name":9,"category_name":49,"show_sort_weight":46,"slug":50},"World Cup","world-cup",{"id":52,"doc_module":4,"doc_module_name":9,"category_name":53,"show_sort_weight":52,"slug":54},10,"Lifestyle","lifestyle",{"id":56,"doc_module":4,"doc_module_name":9,"category_name":57,"show_sort_weight":24,"slug":58},19,"General","general",{"code":4,"msg":60,"data":61},"ok",{"site_id":62,"language":63,"slug":64,"title":65,"keywords":66,"description":67,"schema_data":68,"social_meta":122,"head_meta":124,"extra_data":126,"updated_unix":128},105,"en","can-prions-carry-biological-information-viewpoint","Can Prions Carry Biological Information? - Viewpoint","","The Viewpoint discusses whether prions can carry biological information, contrasting the early-1980s prion hypothesis with molecular, structural, and mechanistic experimental evidence accumulated over four decades. It explains the templating concept of conformational propagation via seeding and describes modern interpretations based on amyloid fibril cross-sectional shapes, elongation, and fission. The article highlights major contradictions and proposes an alternative protein-folding thermodynamics extension to supersaturation-driven aggregation pathways.",{"@graph":69,"@context":121},[70,84,104],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":35,"@type":76,"position":81},"https://docshare.wps.com/document/healthcare/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/can-prions-carry-biological-information-viewpoint/441855/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":98,"encodingFormat":97,"isAccessibleForFree":99,"interactionStatistic":100},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/can-prions-carry-biological-information-viewpoint/441855.png","ImageObject",300,407,{"name":92,"@type":93},"Nguyễn Văn Học","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-09-29",true,{"@type":101,"interactionType":102,"userInteractionCount":4},"InteractionCounter",{"@type":103},"ViewAction",{"@type":105,"mainEntity":106},"FAQPage",[107,113,117],{"name":108,"@type":109,"acceptedAnswer":110},"What mechanism of information transfer does the prion hypothesis propose?","Question",{"text":111,"@type":112},"It proposes conformational propagation through templating, where a prion template imprints its corrupted conformation onto similar proteins via templated elongation and self-propagation.","Answer",{"name":114,"@type":109,"acceptedAnswer":115},"How does the article define “conformational information” in prion templating?",{"text":116,"@type":112},"It links “conformational information” to the specific 2D cross-sectional shape of amyloid fibrils, including the folds and turns of protofilaments and fibrils.",{"name":118,"@type":109,"acceptedAnswer":119},"Why does the article argue that templating fails during amyloid growth?",{"text":120,"@type":112},"It cites evidence that amyloid growth quickly becomes dominated by branching/secondary nucleation, preventing sustained preservation of cross-sectional shape information, and that seeding can drive aggregation without the sequence homology required for parallel in-register stacking.","https://schema.org",{"og:url":83,"og:type":123,"og:title":65,"og:site_name":95,"og:description":67},"article",{"robots":125,"canonical":83},"index,follow",{"doc_id":127,"site_id":62},441855,1790697849,{"code":4,"msg":5,"data":130},{"doc_id":127,"user_id":131,"nickname":92,"user_avatar":132,"doc_module":4,"category_id":34,"category_name":35,"doc_title":65,"doc_description":67,"doc_content":133,"file_id":134,"file_url":135,"file_type":136,"file_size":137,"view_count":4,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":19,"language":138,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":139,"faqs":140,"seo_title":141,"seo_description":67,"update_tm":128,"read_time":52},1374402739827,"https://ap-avatar.wpscdn.com/avatar/14000c97e7351f1a627?x-image-process=image/resize,m_fixed,w_180,h_180&k=1787885694763230660","This article is licensed under CC-BY-NC-ND 4.0   \n[http://pubs.acs.org/journal/acsodf](http://pubs.acs.org/journal/acsodf)  Viewpoint   \nCan Prions Carry Biological Information?  \nKariem Ezzat* and Alberto J. Espay  \n Cite This: ACS Omega 2025, 10, 57842−57845  \nRead Online  \n\n|  |  |  |  |\n| --- | --- | --- | --- |\n| ACCESS   | Metrics & More |  |  Article Recommendations |\n\nABSTRACT: The discovery of the structure of DNA and the elucidation of the molecular mechanisms of replication, transcription, and translation are the foundations of modern biology and medicine. However, in the early 80s, the prion hypothesis introduced a new system of biological information transfer that does not rely on DNA; it introduced the concept of conformational propagation through templating. Unlike the molecular biology revolution, which was based on detailed molecular structures and mechanisms, the prion hypothesis was postulated in the absence of clear molecular structures or mechanisms. In this Viewpoint, we highlight 10 points in which the prion hypothesis contradicts the molecular, structural, and mechanistic experimental evidence accrued since its inception four decades ago.  \nAlternatively, we postulate that an extension of the thermodynamic hypothesis of protein folding (Anfinsen’s dogma) to the state of proteins at high concentration (supersaturation) is better suited for explaining the different facets and pathways of protein aggregation.  \nThe prion hypothesis introduced a new system of biological information: conformational information transfer through templating. Unlike normal protein folding, which takes place spontaneously based on the primary sequence information of the protein (the thermodynamic hypothesis of protein folding or Anfinsen’s dogma), the amyloid conformation in diseases such as Creutzfeldt-Jakob disease is postulated to require a conformational template, a prion, which acts as a template to “imprint” its corrupt conformation on similar proteins and become selfpropagating.1,2 Experimentally, the prion hypothesis is based on one phenomenon: seeding. This is when an amyloid fibril fragment, a seed, is added to a concentrated solution of other proteins, and it catalyzes their transformation into amyloids. However, for decades, it has remained unclear what exactly is the conformational information carried by prions and what is the molecular mechanism of templating. More recently, and thanks to a better understanding of the structure of amyloid fibrils via cryoelectron microscopy, the term “conformational information” has come to designate the specific 2D cross-sectional shape, i.e., the particular cross-sectional pattern of folds and turns of protofilaments and fibrils (Figure 1A) .3 In this framework, a prion, which is an amyloid fibril fragment, templates its cross-sectional shape on incoming protein molecules binding to its tip during elongation. The incoming molecules must accommodate the cross-sectional shape of the fibril by binding in a parallel, in-register manner (i.e., the N and C termini align in the same direction and each amino acid ofthe incoming molecule stacks on top of the identical residue at the tip of the fibril).4 This is also the underlying principle behind the concept of prion “strains”, where different cross-sectional seed  \nshapes are postulated to imprint their distinctive pattern of foldsand turns on incoming protein molecules, leading to different disease phenotypes.3 Similarly, prion propagation occurs via breakage or fission of a fibril with a particular cross-sectional shape into smaller fragments or seeds, which then template their shape onto incoming protein molecules. Thus, in its modern formulation, the prion templating and propagation of conformational information are based on elongation and fission.  \nHowever, for the elongation and fission mechanism topreserve and propagate specific cross-sectional shape information sustainably across generations offibrils and across different cells,","cbCaiv5TMNy6X34o","https://ap.wps.com/l/cbCaiv5TMNy6X34o","pdf",3280246,"English","# Viewpoint: Can Prions Carry Biological Information?\n## Background: DNA replication/transcription/translation vs prion templating\n## Modern prion hypothesis: conformational information, elongation, fission\n## Seeding and conformational information definition from amyloid structure\n## Criteria for templating and experimental challenges\n## Evidence against cross-sectional shape templating via branching and cross-seeding","[{\"question\":\"What mechanism of information transfer does the prion hypothesis propose?\",\"answer\":\"It proposes conformational propagation through templating, where a prion template imprints its corrupted conformation onto similar proteins via templated elongation and self-propagation.\"},{\"question\":\"How does the article define “conformational information” in prion templating?\",\"answer\":\"It links “conformational information” to the specific 2D cross-sectional shape of amyloid fibrils, including the folds and turns of protofilaments and fibrils.\"},{\"question\":\"Why does the article argue that templating fails during amyloid growth?\",\"answer\":\"It cites evidence that amyloid growth quickly becomes dominated by branching/secondary nucleation, preventing sustained preservation of cross-sectional shape information, and that seeding can drive aggregation without the sequence homology required for parallel in-register stacking.\"}]","Can Prions Carry Biological Information? - Viewpoint | PDF"]