{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T09:42:59Z","timestamp":1790934179759,"version":"4.1.0"},"reference-count":18,"publisher":"Microbiology Society","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,1,1]]},"abstract":"<jats:p>In Creutzfeldt\u2013Jakob disease (CJD), the type (type 1 or 2) of abnormal isoform of the prion protein (PrP<jats:sup>Sc<\/jats:sup>) in the brain and the genotype at codon 129 of the PrP gene are major determinants of clinicopathological phenotype. Little is known about the difference in biochemical properties between the two types of PrP<jats:sup>Sc<\/jats:sup>, except for the different proteinase K cleavage sites. To investigate the size of aggregates formed by PrP<jats:sup>Sc<\/jats:sup> types 1 and 2, brain homogenates from various cases of CJD with the same genotype (homozygous for methionine at codon 129) were passed through filters with a mean pore size of 72\u00b14\u2005nm. Type 2 PrP<jats:sup>Sc<\/jats:sup> was efficiently removed from the filtrates by the filters, in contrast to type 1. Even type 2 PrP<jats:sup>Sc<\/jats:sup> from a patient without amyloid plaques was removed more efficiently than type 1 from patients with amyloid plaques. These results indicate that type 2 PrP<jats:sup>Sc<\/jats:sup> has a larger aggregation size than type 1, irrespective of the existence of amyloid plaques.<\/jats:p>","DOI":"10.1099\/vir.0.80389-0","type":"journal-article","created":{"date-parts":[[2004,12,16]],"date-time":"2004-12-16T21:33:06Z","timestamp":1103232786000},"page":"237-240","source":"Crossref","is-referenced-by-count":18,"title":["Type 1 and type 2 human PrPSc have different aggregation sizes in methionine homozygotes with sporadic, iatrogenic and variant Creutzfeldt\u2013Jakob disease"],"prefix":"10.1099","volume":"86","author":[{"given":"Atsushi","family":"Kobayashi","sequence":"first","affiliation":[{"name":"Division of CJD Science and Technology, Department of Prion Research, Center for Translational and Advanced Animal Research on Human Diseases, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sakae","family":"Satoh","sequence":"additional","affiliation":[{"name":"Planova Division, Asahi Kasei Pharma Corporation, Tokyo, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James W.","family":"Ironside","sequence":"additional","affiliation":[{"name":"National Creutzfeldt\u2013Jakob Disease Surveillance Unit, Division of Pathology, University of Edinburgh, Western General Hospital, Edinburgh, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shirou","family":"Mohri","sequence":"additional","affiliation":[{"name":"Laboratory of Biomedicine, Center of Biomedical Research, Graduate School of Medical Sciences, Kyusyu University, Fukuoka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tetsuyuki","family":"Kitamoto","sequence":"additional","affiliation":[{"name":"Division of CJD Science and Technology, Department of Prion Research, Center for Translational and Advanced Animal Research on Human Diseases, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1056\/NEJM198501103120202","article-title":"Creutzfeldt\u2013Jakob disease prion proteins in human brains","volume":"312","author":"Bockman","year":"1985","journal-title":"N Engl J Med"},{"key":"R2","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1038\/383685a0","article-title":"Molecular analysis of prion strain variation and the aetiology of \u2018new variant\u2019 CJD","volume":"383","author":"Collinge","year":"1996","journal-title":"Nature"},{"key":"R3","first-page":"1285","article-title":"Abnormal isoform of prion proteins accumulates in the synaptic structures of the central nervous system in patients with Creutzfeldt\u2013Jakob disease","volume":"140","author":"Kitamoto","year":"1992","journal-title":"Am J Pathol"},{"key":"R4","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1006\/bbrc.1993.1275","article-title":"Novel missense variants of prion protein in Creutzfeldt\u2013Jakob disease or Gerstmann\u2013Str\u00e4ussler syndrome","volume":"191","author":"Kitamoto","year":"1993","journal-title":"Biochem Biophys Res Commun"},{"key":"R5","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1002\/ana.410390613","article-title":"Molecular basis of phenotypic variability in sporadic Creutzfeldt\u2013Jakob disease","volume":"39","author":"Parchi","year":"1996","journal-title":"Ann Neurol"},{"key":"R6","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1038\/386232a0","article-title":"Typing prion isoforms","volume":"386","author":"Parchi","year":"1997","journal-title":"Nature"},{"key":"R7","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1002\/1531-8249(199908)46:2<224::AID-ANA12>3.0.CO;2-W","article-title":"Classification of sporadic Creutzfeldt\u2013Jakob disease based on molecular and phenotypic analysis of 300 subjects","volume":"46","author":"Parchi","year":"1999","journal-title":"Ann Neurol"},{"key":"R8","doi-asserted-by":"crossref","first-page":"10168","DOI":"10.1073\/pnas.97.18.10168","article-title":"Genetic influence on the structural variations of the abnormal prion protein","volume":"97","author":"Parchi","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R9","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/0092-8674(83)90168-X","article-title":"Scrapie prions aggregate to form amyloid-like birefringent rods","volume":"35","author":"Prusiner","year":"1983","journal-title":"Cell"},{"key":"R10","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/S0092-8674(00)81163-0","article-title":"Prion protein biology","volume":"93","author":"Prusiner","year":"1998","journal-title":"Cell"},{"key":"R11","doi-asserted-by":"crossref","first-page":"2173","DOI":"10.1212\/WNL.53.9.2173","article-title":"Sporadic Creutzfeldt\u2013Jakob disease: co-occurrence of different types of PrPSc in the same brain","volume":"53","author":"Puoti","year":"1999","journal-title":"Neurology"},{"key":"R12","doi-asserted-by":"crossref","first-page":"2885","DOI":"10.1099\/vir.0.19236-0","article-title":"Association of an 11\u201312\u2005kDa protease-resistant prion protein fragment with subtypes of dura graft-associated Creutzfeldt\u2013Jakob disease and other prion diseases","volume":"84","author":"Satoh","year":"2003","journal-title":"J Gen Virol"},{"key":"R13","doi-asserted-by":"crossref","first-page":"2585","DOI":"10.1016\/S0002-9440(10)63613-9","article-title":"Humanized knock-in mice expressing chimeric prion protein showed varied susceptibility to different human prions","volume":"163","author":"Taguchi","year":"2003","journal-title":"Am J Pathol"},{"key":"R14","doi-asserted-by":"crossref","first-page":"357","DOI":"10.5360\/membrane.18.357","article-title":"Removal of causative agent of Creutzfeldt\u2013Jakob disease (CJD) through membrane filtration method","volume":"18","author":"Tateishi","year":"1993","journal-title":"Membrane"},{"key":"R15","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1007\/978-94-011-0437-1_99","article-title":"Removal of the prion protein using validatable filter (BMM\u00ae","volume-title":"In Animal Cell Technology: Development Towards the 21st Century","author":"Tateishi","year":"1995"},{"key":"R16","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1006\/biol.2001.0269","article-title":"Scrapie removal using Planova\u00ae virus removal filters","volume":"29","author":"Tateishi","year":"2001","journal-title":"Biologicals"},{"key":"R17","doi-asserted-by":"crossref","first-page":"12868","DOI":"10.1021\/bi025958g","article-title":"Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes","volume":"41","author":"Tzaban","year":"2002","journal-title":"Biochemistry"},{"key":"R18","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1046\/j.1537-2995.2002.00160.x","article-title":"Removal of prion challenge from an immune globulin preparation by use of a size-exclusion filter","volume":"42","author":"Van Holten","year":"2002","journal-title":"Transfusion"}],"container-title":["Journal of General Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/jgv\/10.1099\/vir.0.80389-0?crawler=true","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,10,22]],"date-time":"2020-10-22T20:20:20Z","timestamp":1603398020000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/jgv\/10.1099\/vir.0.80389-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,1,1]]},"references-count":18,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2005,1,1]]}},"URL":"https:\/\/doi.org\/10.1099\/vir.0.80389-0","relation":{},"ISSN":["0022-1317","1465-2099"],"issn-type":[{"value":"0022-1317","type":"print"},{"value":"1465-2099","type":"electronic"}],"subject":[],"published":{"date-parts":[[2005,1,1]]}}}