{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,8,6]],"date-time":"2024-08-06T01:42:46Z","timestamp":1722908566067},"reference-count":13,"publisher":"Microbiology Society","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2004,6,1]]},"abstract":"<jats:p>Assays for the agent of Creutzfeldt\u2013Jakob disease (CJD) include measurement of infectivity in different animal systems, such as wild-type or transgenic mice, and detection of PrP<jats:sup>Sc<\/jats:sup> by different methods and formats. The various assays could be best calibrated against each other by use of uniform readily available materials, and samples of four human brains, two from sporadic CJD patients, one from a variant CJD patient and one from a non-CJD patient, have been prepared as 10\u200a% homogenates dispensed in 2000 vials each for this purpose. Results of <jats:italic>in vitro<\/jats:italic> methods, particularly immunoblot assays, were compared in the first collaborative study described here. While dilution end-points varied, the minimum detectable volume was surprisingly uniform for most assays and differences in technical procedure, other than the sample volume tested, had no detectable systematic effect. The two specimens from sporadic CJD cases contained both type 1 and type 2 prion proteins in approximately equal proportions. The materials have been given the status of reference reagents by the World Health Organization and are available for further study and assessment of other <jats:italic>in vitro<\/jats:italic> or <jats:italic>in vivo<\/jats:italic> assay procedures.<\/jats:p>","DOI":"10.1099\/vir.0.79959-0","type":"journal-article","created":{"date-parts":[[2004,5,27]],"date-time":"2004-05-27T16:48:15Z","timestamp":1085676495000},"page":"1777-1784","source":"Crossref","is-referenced-by-count":42,"title":["Standards for the assay of Creutzfeldt\u2013Jakob disease specimens"],"prefix":"10.1099","volume":"85","author":[{"given":"P.","family":"Minor","sequence":"first","affiliation":[{"name":"NIBSC, Blanche Lane, South Mimms, Potters Bar EN6 3QG, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J.","family":"Newham","sequence":"additional","affiliation":[{"name":"National Transfusion Microbiology Reference Lab, National Blood Service, Colindale Avenue, London NW9 5BG, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"N.","family":"Jones","sequence":"additional","affiliation":[{"name":"NIBSC, Blanche Lane, South Mimms, Potters Bar EN6 3QG, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C.","family":"Bergeron","sequence":"additional","affiliation":[{"name":"University of Toronto, CRND, Tanz Building, 6 Queen's Park Crescent, West Toronto, Ontario, Canada, M5S 3H2"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L.","family":"Gregori","sequence":"additional","affiliation":[{"name":"VA Medical Centre, Mailstop 151, Room 3C-128, 10N Green Street, Baltimore, MD 21201, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D.","family":"Asher","sequence":"additional","affiliation":[{"name":"FDA CBER, Division of Emerging and Transfusion-transmitted Diseases, OBRR, CBER, FDA HFM310, 1401 Rockville Pike, Rockville, MD 20852-1448, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F.","family":"van Engelenburg","sequence":"additional","affiliation":[{"name":"Sanquin Research, Plesmanlaan 125, PO BOX 9190, 1066 AD Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"T.","family":"Stroebel","sequence":"additional","affiliation":[{"name":"Institute of Neurology, Medical University of Vienna, Austrian Reference Centre for Human Prion Diseases, AKH 4J, A-1097 Vienna, Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.","family":"Vey","sequence":"additional","affiliation":[{"name":"Aventis Behring GmbH, Postfach 1230, 35002 Marburg, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Barnard","sequence":"additional","affiliation":[{"name":"Department of Clinical Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge CB3 0EG, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.","family":"Head","sequence":"additional","affiliation":[{"name":"National Creutzfeldt\u2013Jakob Disease Surveillance Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"name":"the WHO Working Group on International Reference Materials for the Diagnosis and Study of Transmissible Spongiform Encephalopathies","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/1522-7243(200011\/12)15:6<357::AID-BIO621>3.0.CO;2-V","article-title":"The measurement of prion protein in bovine brain tissue using differential extraction and DELFIA as a diagnostic test for BSE","volume":"15","author":"Barnard","year":"2000","journal-title":"Luminescence"},{"key":"R2","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1099\/vir.0.18996-0","article-title":"Improved conformation-dependent immunoassay: suitability for human prion detection with enhanced sensitivity","volume":"84","author":"Bellon","year":"2003","journal-title":"J Gen Virol"},{"key":"R3","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1038\/383685a0","article-title":"Molecular analysis of prion strain variation and the aetiology of new variant CJD","volume":"383","author":"Collinge","year":"1996","journal-title":"Nature"},{"key":"R4","doi-asserted-by":"crossref","first-page":"3688","DOI":"10.1128\/JVI.61.12.3688-3693.1987","article-title":"Mouse polyclonal and monoclonal antibody to scrapie-associated fibril protein","volume":"61","author":"Kascsak","year":"1987","journal-title":"J Virol"},{"key":"R5","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/36337","article-title":"Prion (PrPSc)-specific epitope defined by a monoclonal antibody","volume":"390","author":"Korth","year":"1997","journal-title":"Nature"},{"key":"R6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1750-3639.2002.tb00417.x","article-title":"Immunohistochemistry for the prion protein: comparison of different monoclonal antibodies in human prion disease subtypes","volume":"12","author":"Kovacs","year":"2002","journal-title":"Brain Pathol"},{"key":"R7","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/352340a0","article-title":"Homozygous prion protein genotype predisposes to sporadic Creutzfeldt\u2013Jakob disease","volume":"352","author":"Palmer","year":"1991","journal-title":"Nature"},{"key":"R8","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1002\/ana.410390613","article-title":"Molecular basis of phenotypic variability in sproradic Creutzfeldt\u2013Jakob disease","volume":"39","author":"Parchi","year":"1996","journal-title":"Ann Neurol"},{"key":"R9","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1126\/science.1675487","article-title":"Molecular biology of prion diseases","volume":"252","author":"Prusiner","year":"1991","journal-title":"Science"},{"key":"R10","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1126\/science.278.5336.245","article-title":"Prion disease and the BSE crisis","volume":"278","author":"Prusiner","year":"1997","journal-title":"Science"},{"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":"1157","DOI":"10.1038\/2654","article-title":"Eight prion strains have PrPSc molecules with different conformations","volume":"4","author":"Safar","year":"1998","journal-title":"Nat Med"},{"key":"R13","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1038\/9030","article-title":"Strain-specific prion-protein conformation determined by metal ions","volume":"1","author":"Wadsworth","year":"1999","journal-title":"Nat Cell Biol"}],"container-title":["Journal of General Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/jgv\/10.1099\/vir.0.79959-0?crawler=true","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,10,6]],"date-time":"2020-10-06T10:34:05Z","timestamp":1601980445000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/jgv\/10.1099\/vir.0.79959-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,6,1]]},"references-count":13,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2004,6,1]]}},"URL":"https:\/\/doi.org\/10.1099\/vir.0.79959-0","relation":{},"ISSN":["0022-1317","1465-2099"],"issn-type":[{"type":"print","value":"0022-1317"},{"type":"electronic","value":"1465-2099"}],"subject":[],"published":{"date-parts":[[2004,6,1]]}}}