100
Views
6
CrossRef citations to date
0
Altmetric
Original Research

Novel prion mutation (p.Tyr225Cys) in a Korean patient with atypical Creutzfeldt–Jakob disease

, , , , &
Pages 1387-1397 | Published online: 02 Aug 2019

References

  • Mastrianni JA, Iannicola C, Myers RM, DeArmond S, Prusiner SB. Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease. Neurology. 1996;47:1305–1312. doi:10.1212/wnl.47.5.13058909447
  • Escandón-Vargas K, Zorrilla-Vaca A, Corral-Prado RH. Positive 14-3-3 and tau proteins in a sporadic Creutzfeldt-Jakob disease case and a brief perspective of prion diseases in Colombia. Biomedica. 2016;36:29–36. doi:10.7705/biomedica.v36i3.2729
  • Brown K, Mastrianni JA. The prion diseases. J Geriatr Psychiatry Neurol. 2010;23:277–298. doi:10.1177/089198871038357620938044
  • Kübler E, Oesch B, Raeber AJ. Diagnosis of prion diseases. Br Med Bull. 2003;66:267–279. doi:10.1093/bmb/66.1.26714522864
  • Mastrianni JA. The genetics of prion diseases. Genet Med. 2010;12:187–195. doi:10.1097/GIM.0b013e3181cd737420216075
  • Shen L, Ji HF. Mutation directional selection sheds light on prion pathogenesis. Biochem Biophys Res Commun. 2011;410:159–163. doi:10.1016/j.bbrc.2011.06.00721679685
  • Jeong BH, Ju WK, Huh K, et al. Molecular analysis of prion protein gene (PRNP) in Korean patients with Creutzfeldt-Jakob disease. J Korean Med Sci. 1998;13:234–240. doi:10.3346/jkms.1998.13.3.2759681800
  • Marcon G, Indaco A, Di Fede G, et al. Panencephalopathic Creutzfeldt-Jakob disease with distinct pattern of prion protein deposition in a patient with D178N mutation and homozygosity for valine at codon 129 of the prion protein gene. Brain Pathol. 2014;24:148–151. doi:10.1111/bpa.1209524118545
  • Deguchi K, Takamiya M, Deguchi S, et al. Spreading brain lesions in a familial Creutzfeldt-Jakob disease with V180I mutation over 4 years. BMC Neurol. 2012;12:144. doi:10.1186/1471-2377-12-14423176099
  • Mastrianni JA, Capellari S, Telling GC, et al. Inherited prion disease caused by the V210I mutation: transmission to transgenic mice. Neurology. 2001;57:2198–2205. doi:10.1212/wnl.57.12.219811756597
  • Jansen C, Parchi P, Capellari S, et al. Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP. Acta Neuropathol. 2010;119:189–197. doi:10.1007/s00401-009-0609-x19911184
  • Lim JG, Oh E, Park S, Kim YS, Lee A. Familial Creutzfeldt-Jakob disease with M232R mutation presented with corticobasal syndrome. Neurol Sci. 2015;36:1291–1293. doi:10.1007/s10072-014-2038-425515787
  • Shi Q, Zhou W, Chen C, et al. Rare E196A mutation in PRNP gene of 3 Chinese patients with Creutzfeldt-Jacob disease. Prion. 2016;10:331–337. doi:10.1080/19336896.2016.119089727310471
  • Kim MO, Cali I, Oehler A, et al. Genetic CJD with a novel E200G mutation in the prion protein gene and comparison with E200K mutation cases. Acta Neuropathol Commun. 2013;1:80. doi:10.1186/2051-5960-1-8024330864
  • Sanchez-Juan P, Green A, Ladogana A, et al. CSF tests in the differential diagnosis of Creutzfeldt-Jakob disease. Neurology. 2006;67:637–643. doi:10.1212/01.wnl.0000230159.67128.0016924018
  • Giau VV, An SS, Bagyinszky E, Kim SY. Gene panels and primers for next generation sequencing studies on neurodegenerative disorders. Mol Cell Toxicol. 2015;11:89–143. doi:10.1007/s13273-015-0011-9
  • Mackenzie G, Will R. Creutzfeldt-Jakob disease: recent developments. F1000Res. 2017;6:2053. doi:10.12688/f1000research.12681.1
  • Minikel EV, Vallabh SM, Lek M. Quantifying prion disease penetrance using large population control cohorts. Sci Transl Med. 2016;8:322ra9. doi:10.1126/scitranslmed.aaf0746
  • Adzhubei IA, Schmidt S, Peshkin L, et al. A method and server for predicting damaging missense mutations. Nat Method. 2010;7:248–249. doi:10.1038/nmeth0410-248
  • Ng PC, Henikoff S. SIFT: predicting amino acid changes that affect protein function. Nucleic Acids Res. 2003;31:3812–3814. doi:10.1093/nar/gkg50912824425
  • Källberg M, Wang H, Wang S, et al. Template-based protein structure modeling using the RaptorX web server. Nat Protoc. 2012;7:1511–1522. doi:10.1038/nprot.2012.08522814390
  • Ilc G, Giachin G, Jaremko M, et al. NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features. PLoS One. 2010;5:e11715. doi:10.1371/journal.pone.001171520661422
  • Mok TH, Koriath C, Jaunmuktane Z, et al. Evaluating the causality of novel sequence variants in the prion protein gene by example. Neurobiol Aging. 2018;71:265.e1–265.e7. doi:10.1016/j.neurobiolaging.2018.05.011
  • Amano Y, Kimura N, Hanaoka T, et al. Creutzfeldt-Jakob disease with a prion protein gene codon 180 mutation presenting asymmetric cortical high-intensity on magnetic resonance imaging. Prion. 2015;9:29–33. doi:10.1080/19336896.2015.101770325730397
  • Bagyinszky E, Giau VV, Youn YC, An SSA, Kim SY. Characterization of mutations in PRNP (prion) gene and their possible roles in neurodegenerative diseases. Neuropsychiatr Dis Treat. 2018;14:2067–2085. doi:10.2147/NDT.S16544530147320
  • Yeo MJ, Lee SH, Lee SY, et al. Familial Creutzfeldt-Jakob disease with a mutation at codon 180 presenting with an atypical phenotype. J Clin Neurosci. 2013;20:180–182. doi:10.1016/j.jocn.2012.01.04422999564
  • Jin K, Shiga Y, Shibuya S, et al. Clinical features of Creutzfeldt-Jakob disease with V180I mutation. Neurology. 2004;62:502–505. doi:10.1212/01.wnl.0000106954.54011.8014872044
  • Clerici F, Elia A, Girotti F, et al. Atypical presentation of Creutzfeldt-Jakob disease: the first Italian case associated with E196K mutation in the PRNP gene. J Neurol Sci. 2008;275:145–147. doi:10.1016/j.jns.2008.06.03618706660
  • Cali I, Mikhail F, Qin K, et al. Impaired transmissibility of atypical prions from genetic CJD G114V. Neurol Genet. 2018;4:e253. doi:10.1212/NXG.000000000000025330109268
  • Brown P, Goldfarb LG, McCombie WR, et al. Atypical Creutzfeldt-Jakob disease in an American family with an insert mutation in the PRNP amyloid precursor gene. Neurology. 1992;42:422–427. doi:10.1212/wnl.42.2.4221736177
  • Kapaki E, Kilidireas K, Paraskevas GP, Michalopoulou M, Patsouris E. Highly increased CSF tau protein and decreased beta-amyloid (1–42) in sporadic CJD: a discrimination from alzheimer’s disease? J Neurol Neurosurg Psychiatry. 2001;71:401–403. doi:10.1136/jnnp.71.3.40111511720
  • Mollenhauer B, Esselmann H, Roeber S, et al. Different CSF β-amyloid processing in alzheimer’s and Creutzfeldt-Jakob disease. J Neural Transm (Vienna). 2011;118:691–697. doi:10.1007/s00702-010-0543-z21210287
  • Chi NF, Lee YC, Lu YC, Wu HM, Soong BW. Transmissible spongiform encephalopathies with P102L mutation of PRNP manifesting different phenotypes: clinical, neuroimaging, and electrophysiological studies in Chinese kindred in Taiwan. J Neurol. 2010;257:191–197. doi:10.1007/s00415-009-5290-419696976
  • Rosenthal NP, Keesey J, Crandall B, Brown WJ. Familial neurological disease associated with spongiform encephalopathy. Arch Neurol. 1976;33:252–259.769760
  • Gambetti P, Kong Q, Zou W, Parchi P, Chen SG. Sporadic and familial CJD: classification and characterisation. Br Med Bull. 2003;66:213–239. doi:10.1093/bmb/66.1.21314522861
  • Gendoo DM, Harrison PM. The landscape of the prion protein’s structural response to mutation revealed by principal component analysis of multiple NMR ensembles. PLoS Comput Biol. 2012;8:e1002646. doi:10.1371/journal.pcbi.100264622912570
  • Hermann LM, Caughey B. The importance of the disulfide bond in prion protein conversion. Neuroreport. 1998;9:2457–2461. doi:10.1097/00001756-199808030-000069721914
  • Maiti NR, Surewicz WK. The role of disulfide bridge in the folding and stability of the recombinant human prion protein. J Biol Chem. 2001;276(4):2427–2431. doi:10.1074/jbc.M00786220011069909
  • Mossuto MF. Disulfide bonding in neurodegenerative misfolding diseases. Int J Cell Biol. 2013;2013:318319. doi:10.1155/2013/31831923983694
  • Welker E, Wedemeyer WJ, Scheraga HA. A role for intermolecular disulfide bonds in prion diseases? Proc Natl Acad Sci U S A. 2001;98:4334–4336. doi:10.1073/pnas.07106659811274354
  • Li Y, Yan J, Zhang X, Huang K. Disulfide bonds in amyloidogenesis diseases related proteins. Proteins. 2013;81:1862–1873. doi:10.1002/prot.2433823760807
  • Dichgans M, Herzog J, Gasser T. NOTCH3 mutation involving three cysteine residues in a family with typical CADASIL. Neurology. 2001;57:1714–1717. doi:10.1212/wnl.57.9.171411706120
  • Arboleda-Velasquez JF, Rampal R, Fung E, et al. CADASIL mutations impair notch3 glycosylation by fringe. Hum Mol Genet. 2005;14:1631–1639. doi:10.1093/hmg/ddi17115857853
  • Woulfe J, Kertesz A, Frohn I, Bauer S, George-Hyslop PS, Bergeron C. Gerstmann-Sträussler-Scheinker disease with the Q217R mutation mimicking frontotemporal dementia. Acta Neuropathol. 2005;110:317–319. doi:10.1007/s00401-005-1054-016025285
  • Alzualde A, Indakoetxea B, Ferrer I, et al. A novel PRNP Y218N mutation in Gerstmann-Sträussler-Scheinker disease with neurofibrillary degeneration. J Neuropathol Exp Neurol. 2010;69:789–800. doi:10.1097/NEN.0b013e3181e8573720613639
  • Kovač V, Zupančič B, Ilc G, Plavec J, Čurin Šerbec V. Truncated prion protein PrP226* – a structural view on its role in amyloid disease. Biochem Biophys Res Commun. 2017;484:45–50. doi:10.1016/j.bbrc.2017.01.07828109886