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2013-03-11Zeitschriftenartikel DOI: 10.1177/0023677213476856
Towards further reduction and replacement of animal bioassays in prion research by cell and protein misfolding cyclic amplification assays
dc.contributor.authorBoerner, Susann
dc.contributor.authorWagenführ, Katja
dc.contributor.authorDaus, Martin L.
dc.contributor.authorThomzig, Achim
dc.contributor.authorBeekes, Michael
dc.date.accessioned2018-05-07T17:33:26Z
dc.date.available2018-05-07T17:33:26Z
dc.date.created2014-03-17
dc.date.issued2013-03-11none
dc.identifier.otherhttp://edoc.rki.de/oa/articles/relvDy2C8NqEQ/PDF/29YuGjA1Aa5A.pdf
dc.identifier.urihttp://edoc.rki.de/176904/1840
dc.description.abstractLaboratory animals have long since been used extensively in bioassays for prions in order to quantify, usually in terms of median infective doses [ID50], how infectious these pathogens are in vivo. The identification of aberrant prion protein as the main component and self-replicating principle of prions has given rise to alternative approaches for prion titration. Such approaches often use protein misfolding cyclic amplification (PMCA) for the cell-free biochemical measurement of prion-associated seeding activity, or cell assays for the titration of in vitro infectivity. However, median seeding and cell culture infective doses (SD50 and CCID50, respectively) of prions are neither formally congruent nor definitely representative for ID50 titres in animals and can be therefore only tentatively translated into the latter. This may potentially impede the acceptance and use of alternative methods to animal bioassays in prion research. Thus, we suggest performing PMCA and cell assays jointly, and to check whether these profoundly different test principles deliver consistent results in order to strengthen the reliability and credibility of prion ID50 assessments by in vitro methods. With regard to this rationale, we describe three pairs of PMCA and glial cell assays for different hamster-adapted prion agents (the frequently used 263K scrapie strain, and 22A-H scrapie and BSE-H). In addition, we report on the adaptation of quantitative PMCA to human variant Creutzfeldt-Jakob disease (vCJD) prions on steel wires for prion disinfection studies. Our rationale and methodology can be systematically extended to other types of prions and used to further reduce or replace prion bioassays in rodents.eng
dc.language.isoeng
dc.publisherRobert Koch-Institut, Infektionskrankheiten / Erreger
dc.subjectAnimalseng
dc.subjectHumanseng
dc.subjectCattleeng
dc.subjectSensitivity and Specificityeng
dc.subjectCreutzfeldt-Jakob Syndrome/metabolismeng
dc.subjectEncephalopathy Bovine Spongiform/metabolismeng
dc.subjectPrPSc Proteins/chemistryeng
dc.subjectPrPSc Proteins/geneticseng
dc.subjectBiological Assay/instrumentationeng
dc.subjectBiological Assay/methodseng
dc.subjectBlotting Westerneng
dc.subjectCattle Diseases/metabolismeng
dc.subjectCricetinaeeng
dc.subjectDisinfection/methodseng
dc.subjectElectrophoresis Polyacrylamide Geleng
dc.subjectNeuroglia/metabolismeng
dc.subjectNeuroglia/pathologyeng
dc.subjectPrPC Proteins/chemistryeng
dc.subjectPrPC Proteins/geneticseng
dc.subjectPrPC Proteins/metabolismeng
dc.subjectPrPSc Proteins/metabolismeng
dc.subjectPrion Diseases/geneticseng
dc.subjectPrion Diseases/metabolismeng
dc.subjectProtein Engineering/instrumentationeng
dc.subjectProtein Engineering/methodseng
dc.subjectProtein Foldingeng
dc.subjectScrapie/metabolismeng
dc.subjectSheep/metabolismeng
dc.subject.ddc610 Medizin
dc.titleTowards further reduction and replacement of animal bioassays in prion research by cell and protein misfolding cyclic amplification assays
dc.typeperiodicalPart
dc.identifier.urnurn:nbn:de:0257-10035869
dc.identifier.doi10.1177/0023677213476856
dc.identifier.doihttp://dx.doi.org/10.25646/1765
local.edoc.container-titleLaboratory Animals
local.edoc.container-textBoerner, S., Wagenfüh, K., Daus, M.L., Thomzig, A., Beekes, M. Towards further reduction and replacement of animal bioassays in prion research by cell and protein misfolding cyclic amplification assays (2013) Laboratory Animals, 47 (2), pp. 106-115.
local.edoc.fp-subtypeArtikel
local.edoc.type-nameZeitschriftenartikel
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-urlhttp://lan.sagepub.com/content/47/2/106
local.edoc.container-publisher-nameSAGE Publications
local.edoc.container-volume47
local.edoc.container-issue2
local.edoc.container-year2013

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