Application of protein misfolding cyclic amplification for the rapid diagnosis of acquired Creutzfeldt-Jakob disease
Main Article Content
Abstract
The susceptibility, clinical phenotype, and pathology of Creutzfeldt-Jakob disease (CJD) depends on both a methionine (M) /valine (V) polymorphism at codon 129 of the PRNP gene and the type of abnormal isoform of prion protein (PrPSc), either type 1 or type 2. The majority of CJD is sporadic CJD (sCJD) or genetic CJD, while CJD can be transmitted resulting in acquired CJD. It has been reported that dura mater graft-associated CJD (dCJD) with methionine homozygosity at codon 129 could be divided into distinct two phenotypes, namely the non-plaque-type of dCJD (np-dCJD) or the plaque-type of dCJD (p-dCJD). The cause of these two distinct phenotypes of dCJD was clarified by animal transmission studies using PrP-humanized mice based on the susceptibility and neurological or biochemical features in the mice inoculated with PrPSc from each dCJD subgroup. It is now likely that np-dCJD is associated with sCJD-MM1 or -MV1, the most common forms of sCJD (denoted as M1 strain in transmission studies), while p-dCJD is associated with sCJD-VV2 or -MV2, the second most common forms of sCJD (denoted as V2 strain). Although animal transmission studies are the most useful tool for identifying such atypical CJDs, relying exclusively on animal transmission studies may not be feasible due to the enormous cost and time. Therefore, we reported a method that can more easily and rapidly distinguish between M1-derived and V2-derived acquired CJDs using the protein misfolding cyclic amplification (PMCA) technique. Here, we describe the advantages of PMCA as a diagnostic tool for acquired CJD based on a comparison with those of conventional animal transmission studies.
Article Details
How to Cite
TAKEUCHI, Atsuko et al.
Application of protein misfolding cyclic amplification for the rapid diagnosis of acquired Creutzfeldt-Jakob disease.
Medical Research Archives, [S.l.], v. 5, n. 4, apr. 2017.
ISSN 2375-1924.
Available at: <https://esmed.org/MRA/mra/article/view/1078>. Date accessed: 20 apr. 2024.
Keywords
Creutzfeldt-Jakob disease; Prion protein; Dura mater grafts; Protein misfolding cyclic amplification; Humanized knock-in mouse
Section
Review Articles
The Medical Research Archives grants authors the right to publish and reproduce the unrevised contribution in whole or in part at any time and in any form for any scholarly non-commercial purpose with the condition that all publications of the contribution include a full citation to the journal as published by the Medical Research Archives.
References
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Bishop MT, Will RG, Manson JC. Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties. Proc Natl Acad Sci U S A. 2010; 107 (26): 12005–12010. [PubMed: 20547859]
Brown P, Brandel JP, Preece M, et al. Iatrogenic Creutzfeldt-Jakob disease: the waning of an era. Neurology. 2006; 67 (3): 389–393. [PubMed: 16855204]
Brown P, Brandel JP, Sato T, et al. Iatrogenic Creutzfeldt-Jakob Disease, Final Assessment. Emerg Infect Dis. 2012; 18 (6): 901–907. [PubMed: 22607808]
Bruce ME, Will RG, Ironside JW, et al. Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature. 1997; 389 (6650): 498–501. [PubMed: 9333239]
Cali I, Miller CJ, Parisi JE, et al. Distinct pathological phenotypes of Creutzfeldt-Jakob disease in recipients of prion-contaminated growth hormone. Acta Neuropathol Commun. 2015; 3: 37. [PubMed: 26108478]
Castilla J, Saa P, Hetz C, et al. In vitro generation of infectious scrapie prions. Cell. 2005; 121 (2): 195–206. [PubMed: 15851027]
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Castilla J, Morales R, Saa P, et al. Cell-free propagation of prion strains. EMBO J. 2008; 27 (19): 2557–2566. [PubMed: 18800058]
Collinge J, Sidle KC, Meads J, et al. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature. 1996; 383 (6602): 685–690. [PubMed: 8878476]
Diack AB, Head MW, McCutcheon S, et al. Variant CJD. 18 years of research and surveillance. Prion. 2014; 8 (4): 286–295. [PubMed: 25495404]
Green KM, Castilla J, Seward TS, et al. Accelerated high fidelity prion amplification within and across prion species barriers. PLoS Pathog. 2008; 4 (8): e1000139. [PubMed: 18769716]
Hoshi K, Yoshino H, Urata J, et al. Creutzfeldt-Jakob disease associated with cadaveric dura mater grafts in Japan. Neurology. 2000; 55 (5): 718–721. [PubMed: 10980745]
Kobayashi A, Asano M, Mohri S, et al. Cross-sequence transmission of sporadic Creutzfeldt-Jakob disease creates a new prion strain. J Biol Chem. 2007; 282 (41): 30022–30028. [PubMed: 17709374]
Kobayashi A, Asano M, Mohri S, et al. A traceback phenomenon can reveal the origin of prion infection. Neuropathology. 2009; 29 (5): 619–624. [PubMed: 19659941]
Kobayashi A, Sakuma N, Matsuura Y, et al. Experimental verification of a traceback phenomenon in prion infection. J Virol. 2010; 84 (7): 3230–3238. [PubMed: 20089646]
Kobayashi A, Iwasaki Y, Otsuka H, et al. Deciphering the pathogenesis of sporadic Creutzfeldt-Jakob disease with codon 129 M/V and type 2 abnormal prion protein. Acta Neuropathol Commun. 2013; 1:74. [PubMed: 24252157]
Kobayashi A, Matsuura Y, Mohri S, et al. Distinct origins of dura mater graft-associated Creutzfeldt-Jakob disease: past and future problems. Acta Neuropathol Commun. 2014; 2:32. [PubMed: 24685293]
Kobayashi A, Parchi P, Yamada M, et al. Transmission properties of atypical Creutzfeldt-Jakob disease: a clue to disease etiology? J Virol. 2015; 89 (17): 3939–3946. [PubMed: 26085146]
Kretzschmar HA, Sethi S, Foldvari Z, et al. Latrogenic Creutzfeldt-Jakob disease with florid plaques. Brain Pathol. 2003; 13 (3): 245–249. [PubMed: 12946015]
Kurt TD, Perrott MR, Wilusz CJ, et al. Efficient in vitro amplification of chronic wasting disease PrPRES. J Virol. 2007; 81 (17):9605–9608. [PubMed: 17553879]
Lasmezas CI, Deslys JP, Demaimay R, et al. Strain specific and common pathogenic events in murine models of scrapie and bovine spongiform encephalopathy. J Gen Virol. 1996; 77 (Pt 7): 1601–1609. [PubMed: 8758005]
Mochizuki Y, Mizutani T, Tajiri N, et al. Creutzfeldt-Jakob disease with florid plaques after cadaveric dura mater graft. Neuropathology. 2003; 23 (2):136–140. [PubMed: 12777102]
Murayama Y, Yoshioka M, Yokoyama T, et al. Efficient in vitro amplification of a mouse-adapted scrapie prion protein. Neurosci Lett. 2007; 413 (3): 270–273. [PubMed: 17174030]
Murayama Y, Masujin K, Imamura M, et al. Ultrasensitive detection of PrP (Sc) in the cerebrospinal fluid and blood of macaques infected with bovine spongiform encephalopathy prion. J Gen Virol. 2014; 95 (Pt 11): 2576–2588. [PubMed: 25024281]
Oshita M, Yokoyama T, Takei Y, et al. Efficient propagation of variant Creutzfeldt-Jakob disease prion protein using the cell-protein misfolding cyclic amplification technique with samples containing plasma and heparin. Transfusion. 2016; 56 (1): 223–230. [PubMed: 26347231]
Parchi P, Giese A, Capellari S, et al. Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann Neurol. 1999; 46 (2): 224–233. [PubMed: 10443888]
Prusiner SB, Scott MR, DeArmond SJ, et al. Prion protein biology. Cell. 1998; 93 (3): 337–348. [PubMed: 9590169]
Ritchie DL, Barria MA, Peden AH, et al. UK Iatrogenic Creutzfeldt-Jakob disease: investigating human prion transmission across genotypic barriers using human tissue-based and molecular approaches. Acta Neuropathol. 2016; [PubMed: 27812793]
Rudge P, Jaunmuktane Z, Adlard P, et al. Iatrogenic CJD due to pituitary-derived growth hormone with genetically determined incubation times of up to 40 years. Brain. 2015; 138 (Pt 11): 3386–3399. [PubMed: 26268531]
Saborio GP, Permanne B, Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature. 2001; 411 (6839): 810–813. [PubMed: 11459061]
Shimizu S, Hoshi K, Muramoto T, et al. Creutzfeldt-Jakob disease with florid-type plaques after cadaveric dura mater grafting. Arch Neurol. 1999; 56 (3): 357–362. [PubMed: 10190828]
Soto C, Anderes L, Suardi S, et al. Pre-symptomatic detection of prions by cyclic amplification of protein misfolding. FEBS Lett. 2005; 579 (3): 638–642. [PubMed: 15670821]
Takeuchi A, Kobayashi A, Parchi P, et al. Distinctive properties of plaque-type dura mater graft-associated Creutzfeldt-Jakob disease in cell-protein misfolding cyclic amplification. Lab Invest. 2016; 96 (5): 581–587. [PubMed: 26878132]
Will RG, Ironside JW, Zeidler M, et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet. 1996; 347 (9006): 921–925. [PubMed: 8598754]
Yamada M, Noguchi-Shinohara M, Hamaguchi T, et al. Dura mater graft-associated Creutzfeldt-Jakob disease in Japan: clinicopathological and molecular characterization of the two distinct subtypes. Neuropathology. 2009; 29 (5): 609–618. [PubMed: 19659940]
Yokoyama T, Takeuchi A, Yamamoto M, et al. Heparin enhances the cell-protein misfolding cyclic amplification efficiency of variant Creutzfeldt-Jakob disease. Neurosci Lett. 2011; 498 (2): 119 –123. [PubMed: 21565253]
Belondrade M, Nicot S, Beringue V, et al. Rapid and Highly Sensitive Detection of Variant Creutzfeldt-Jakob Disease Abnormal Prion Protein on Steel Surfaces by Protein Misfolding Cyclic Amplification: Application to Prion Decontamination Studies. PLoS One. 2016; 11(1): e0146833. [PubMed: 26800081]
Bishop MT, Will RG, Manson JC. Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties. Proc Natl Acad Sci U S A. 2010; 107 (26): 12005–12010. [PubMed: 20547859]
Brown P, Brandel JP, Preece M, et al. Iatrogenic Creutzfeldt-Jakob disease: the waning of an era. Neurology. 2006; 67 (3): 389–393. [PubMed: 16855204]
Brown P, Brandel JP, Sato T, et al. Iatrogenic Creutzfeldt-Jakob Disease, Final Assessment. Emerg Infect Dis. 2012; 18 (6): 901–907. [PubMed: 22607808]
Bruce ME, Will RG, Ironside JW, et al. Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature. 1997; 389 (6650): 498–501. [PubMed: 9333239]
Cali I, Miller CJ, Parisi JE, et al. Distinct pathological phenotypes of Creutzfeldt-Jakob disease in recipients of prion-contaminated growth hormone. Acta Neuropathol Commun. 2015; 3: 37. [PubMed: 26108478]
Castilla J, Saa P, Hetz C, et al. In vitro generation of infectious scrapie prions. Cell. 2005; 121 (2): 195–206. [PubMed: 15851027]
Castilla J, Saa P, Morales R, etal. Protein misfolding cyclic amplification for diagnosis and prion propagation studies. Methods Enzymol. 2006; 412:3–21. [PubMed: 17046648]
Castilla J, Morales R, Saa P, et al. Cell-free propagation of prion strains. EMBO J. 2008; 27 (19): 2557–2566. [PubMed: 18800058]
Collinge J, Sidle KC, Meads J, et al. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature. 1996; 383 (6602): 685–690. [PubMed: 8878476]
Diack AB, Head MW, McCutcheon S, et al. Variant CJD. 18 years of research and surveillance. Prion. 2014; 8 (4): 286–295. [PubMed: 25495404]
Green KM, Castilla J, Seward TS, et al. Accelerated high fidelity prion amplification within and across prion species barriers. PLoS Pathog. 2008; 4 (8): e1000139. [PubMed: 18769716]
Hoshi K, Yoshino H, Urata J, et al. Creutzfeldt-Jakob disease associated with cadaveric dura mater grafts in Japan. Neurology. 2000; 55 (5): 718–721. [PubMed: 10980745]
Kobayashi A, Asano M, Mohri S, et al. Cross-sequence transmission of sporadic Creutzfeldt-Jakob disease creates a new prion strain. J Biol Chem. 2007; 282 (41): 30022–30028. [PubMed: 17709374]
Kobayashi A, Asano M, Mohri S, et al. A traceback phenomenon can reveal the origin of prion infection. Neuropathology. 2009; 29 (5): 619–624. [PubMed: 19659941]
Kobayashi A, Sakuma N, Matsuura Y, et al. Experimental verification of a traceback phenomenon in prion infection. J Virol. 2010; 84 (7): 3230–3238. [PubMed: 20089646]
Kobayashi A, Iwasaki Y, Otsuka H, et al. Deciphering the pathogenesis of sporadic Creutzfeldt-Jakob disease with codon 129 M/V and type 2 abnormal prion protein. Acta Neuropathol Commun. 2013; 1:74. [PubMed: 24252157]
Kobayashi A, Matsuura Y, Mohri S, et al. Distinct origins of dura mater graft-associated Creutzfeldt-Jakob disease: past and future problems. Acta Neuropathol Commun. 2014; 2:32. [PubMed: 24685293]
Kobayashi A, Parchi P, Yamada M, et al. Transmission properties of atypical Creutzfeldt-Jakob disease: a clue to disease etiology? J Virol. 2015; 89 (17): 3939–3946. [PubMed: 26085146]
Kretzschmar HA, Sethi S, Foldvari Z, et al. Latrogenic Creutzfeldt-Jakob disease with florid plaques. Brain Pathol. 2003; 13 (3): 245–249. [PubMed: 12946015]
Kurt TD, Perrott MR, Wilusz CJ, et al. Efficient in vitro amplification of chronic wasting disease PrPRES. J Virol. 2007; 81 (17):9605–9608. [PubMed: 17553879]
Lasmezas CI, Deslys JP, Demaimay R, et al. Strain specific and common pathogenic events in murine models of scrapie and bovine spongiform encephalopathy. J Gen Virol. 1996; 77 (Pt 7): 1601–1609. [PubMed: 8758005]
Mochizuki Y, Mizutani T, Tajiri N, et al. Creutzfeldt-Jakob disease with florid plaques after cadaveric dura mater graft. Neuropathology. 2003; 23 (2):136–140. [PubMed: 12777102]
Murayama Y, Yoshioka M, Yokoyama T, et al. Efficient in vitro amplification of a mouse-adapted scrapie prion protein. Neurosci Lett. 2007; 413 (3): 270–273. [PubMed: 17174030]
Murayama Y, Masujin K, Imamura M, et al. Ultrasensitive detection of PrP (Sc) in the cerebrospinal fluid and blood of macaques infected with bovine spongiform encephalopathy prion. J Gen Virol. 2014; 95 (Pt 11): 2576–2588. [PubMed: 25024281]
Oshita M, Yokoyama T, Takei Y, et al. Efficient propagation of variant Creutzfeldt-Jakob disease prion protein using the cell-protein misfolding cyclic amplification technique with samples containing plasma and heparin. Transfusion. 2016; 56 (1): 223–230. [PubMed: 26347231]
Parchi P, Giese A, Capellari S, et al. Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann Neurol. 1999; 46 (2): 224–233. [PubMed: 10443888]
Prusiner SB, Scott MR, DeArmond SJ, et al. Prion protein biology. Cell. 1998; 93 (3): 337–348. [PubMed: 9590169]
Ritchie DL, Barria MA, Peden AH, et al. UK Iatrogenic Creutzfeldt-Jakob disease: investigating human prion transmission across genotypic barriers using human tissue-based and molecular approaches. Acta Neuropathol. 2016; [PubMed: 27812793]
Rudge P, Jaunmuktane Z, Adlard P, et al. Iatrogenic CJD due to pituitary-derived growth hormone with genetically determined incubation times of up to 40 years. Brain. 2015; 138 (Pt 11): 3386–3399. [PubMed: 26268531]
Saborio GP, Permanne B, Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature. 2001; 411 (6839): 810–813. [PubMed: 11459061]
Shimizu S, Hoshi K, Muramoto T, et al. Creutzfeldt-Jakob disease with florid-type plaques after cadaveric dura mater grafting. Arch Neurol. 1999; 56 (3): 357–362. [PubMed: 10190828]
Soto C, Anderes L, Suardi S, et al. Pre-symptomatic detection of prions by cyclic amplification of protein misfolding. FEBS Lett. 2005; 579 (3): 638–642. [PubMed: 15670821]
Takeuchi A, Kobayashi A, Parchi P, et al. Distinctive properties of plaque-type dura mater graft-associated Creutzfeldt-Jakob disease in cell-protein misfolding cyclic amplification. Lab Invest. 2016; 96 (5): 581–587. [PubMed: 26878132]
Will RG, Ironside JW, Zeidler M, et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet. 1996; 347 (9006): 921–925. [PubMed: 8598754]
Yamada M, Noguchi-Shinohara M, Hamaguchi T, et al. Dura mater graft-associated Creutzfeldt-Jakob disease in Japan: clinicopathological and molecular characterization of the two distinct subtypes. Neuropathology. 2009; 29 (5): 609–618. [PubMed: 19659940]
Yokoyama T, Takeuchi A, Yamamoto M, et al. Heparin enhances the cell-protein misfolding cyclic amplification efficiency of variant Creutzfeldt-Jakob disease. Neurosci Lett. 2011; 498 (2): 119 –123. [PubMed: 21565253]