Surround optical fiber immunoassay (SOFIA): An ultra-sensitive assay for prion protein detection

Journal of Virological Methods

Volumn 159, Issue 1, 2009, Pages 15-22

  Chang, Binggong ^a   Gray, Perry ^b   Piltch, Martin ^b   Bulgin, Marie S ^c   Sorensen Melson, Sharon ^c   Miller, Michael W ^d   Davies, Paul ^e   Brown, David R ^e   Coughlin, Daniel R ^b   Rubenstein, Richard ^a  

^a SUNY Downstate Medical Center   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

^c UNIVERSITY OF IDAHO   (United States)

^d NATIONAL WILDLIFE RESEARCH CENTER   (United States)

^e University of Bath   (United Kingdom)

Author keywords

Fiber optics; Immunoassay; PrP; SOFIA

Indexed keywords

GLASS FIBER; MONOCLONAL ANTIBODY; PRION PROTEIN; PROTEINASE; RECOMBINANT PROTEIN;

ANIMAL TISSUE; ARTICLE; BRAIN DISEASE; BRAIN TISSUE; CHRONIC WASTING DISEASE; CONTROLLED STUDY; DEER; DILUTION; FLUORESCENCE; HAMSTER; IMMUNOASSAY; MEDICAL TECHNOLOGY; NONHUMAN; PATHOGENESIS; PRION DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; SCRAPIE; SENSITIVITY AND SPECIFICITY; SHEEP; SURROUND OPTICAL FIBER IMMUNOASSAY;

ANIMALS; ANTIBODIES, MONOCLONAL; BLOTTING, WESTERN; BRAIN; CRICETINAE; DEER; FLUORESCENCE; IMMUNOASSAY; OPTICAL FIBERS; PRPSC PROTEINS; SCRAPIE; SENSITIVITY AND SPECIFICITY; SHEEP; WASTING DISEASE, CHRONIC;

CERVIDAE; CRICETINAE; OVIS ARIES;

EID: 67349179480     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jviromet.2009.02.019     Document Type: Article

References (54)

1. Atarashi R., Moore R.A., Sim V.L., Hughson A.G., Dorward D.H., Onwubiko H.A., Priola S.A., and Caughey B. Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat. Methods 4 (2007) 645-650
2. Atarashi R., Wilham J.M., Christensen L., Hughson A.G., Moore R.A., Johnson L.M., Onwubiko H.A., Priola S.A., and Caughey B. Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking. Nat. Methods 5 (2008) 211-212
3. Barron R.M., Thomson V., Jamieson E., Melton D.W., Ironside J., Will R., and Manson J.C. Changing a single amino acid in the N-terminus of murine PrP alters TSE incubation time across three species barriers. EMBO J. 20 (2001) 5070-5078
4. Beekes M., Lasch P., and Naumann D. Analytical applications of Fourier transform-infrared (FT-IR) spectroscopy in microbiology and prion research. Vet. Microbiol. 123 (2007) 305-319
5. Bieschke J., Giese A., Schulz-Schaeffer W., Zerr I., Poser S., Eigen M., and Kretzschmar H. Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 5468-5473
6. Brown D.R., Wong B.-S., Hafiz F., Clive C., Haswell S.J., and Jones I.M. Normal prion protein has an activity like that of superoxide dismutase. Biochem. J. 344 (1999) 1-5
7. Brown P., Cervenakova L., and Diringer H. Blood infectivity and the prospects for a diagnostic screening test in Creutzfeldt-Jakob disease. J. Lab. Clin. Med. 137 (2001) 5-13
8. Castilla J., Saá P., Hetz C., and Soto C. In vitro generation of infectious scrapie prions. Cell 121 (2005) 195-206
9. Chang B., Cheng X., Yin S., Pan T., Zhang H., Wong P., Kang S.-C., Xiao F., Yan H., Li C., Wolfe L.L., Miller M.W., Wisniewski T., Greene M.I., and Sy M.-S. Test for detection of disease-associated prion aggregate in the blood of infected but asymptomatic animals. Clin. Vaccine Immunol. 14 (2007) 36-43
10. Chang B., Miller M.W., Bulgin M.S., Sorenson-Melson S., Balachandran A., Chiu A., and Rubenstein R. PrP antibody binding-induced epitope modulation evokes immunocooperativity. J. Neuroimmunol. 205 (2008) 94-100
11. Collins S., Boyd A., Fletcher A., Gonzales M.F., McLean C.A., and Masters C.L. Recent advances in the pre-mortem diagnosis of Creutzfeldt-Jakob disease. J. Clin. Neurosci. 7 (2002) 195-202
12. DeArmond S.J., Mobley W.C., DeMott D.L., Barry R.A., Beckstead J.H., and Prusiner S.B. Changes in the localization of brain prion proteins during scrapie infection. Neurology 37 (1987) 1271-1280
13. Deleault N.R., Harris B.T., Rees J.R., and Supattapone S. Formation of native prions from minimal components in vitro. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 9741-9746
14. Everest D.J., Waterhouse S., Kelly T., Velo-Rego E., and Sauer M.J. Effectiveness of capillary electrophoresis fluoroimmunoassay of blood PrpSc for evaluation of scrapie pathogenesis in sheep. J. Vet. Diag. Invest. 19 (2007) 552-557
15. Fujii F., Horiuchi M., Ueno M., Sakata H., Nagao I., Tamura M., and Kinjo M. Detection of prion protein immune complex for bovine spongiform encephalopathy diagnosis using fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy. Anal. Biochem. 370 (2007) 131-141
16. Ingrosso L., Vetrugno V., Cardone F., and Pocchiari M. Molecular diagnostics of transmissible spongiform encephalopathies. Trends Mol. Med. 8 (2002) 273-280
17. Jackman R., Everest D.J., Schmerr M.J., Khawaja M., Keep P., and Docherty J. Evaluation of a preclinical blood test for scrapie in sheep using immunocapillary electrophoresis. J. AOAC Int. 89 (2006) 720-727
18. Jackman R., and Schmerr M.J. Analysis of the performance of antibody capture methods using fluorescent peptides with capillary zone electrophoresis with laser induced fluorescence. Electrophoresis 24 (2003) 892-896
19. Jendroska K., Heinzel F.P., Torchia M., Stowring L., Kretzschmar H.A., Kon A., Stern A., Prusiner S.B., and DeArmond S.J. Proteinase-resistant prion protein accumulation in Syrian hamster brain correlates with regional pathology and scrapie infectivity. Neurology 41 (1991) 1482-1490
20. 111 induces β-sheet formation in the unstructured amyloidogenic region of the prion protein. J. Biol. Chem. 279 (2004) 32018-32027
21. Jones M., Peden A., Prowse C., Gröner A., Manson J., Turner M., Ironside J., Macgregor I., and Head M. In vitro amplification and detection of variant Creutzfeldt-Jakob disease PrPSc. J. Pathol. 213 (2007) 21-26
22. Kascsak R.J., Rubenstein R., Merz P.A., Tonna-DeMasi M., Fersko R., Carp R.I., Wisniewski H.W., and Diringer H. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J. Virol. 61 (1987) 3688-3693
23. Kim J.-L., Wang C., Kuizon S., Xu J., Barengolts D., Gray P.C., and Rubenstein R. Simple and specific detection of abnormal prion protein by a magnetic bead-based immunoassay coupled with laser-induced fluorescence spectrofluorometry. J. Neuroimmunol. 158 (2005) 112-119
24. Klohn P.C., Stoltze L., Flechsig E., Enari M., and Weissmann C. A quantitative, highly sensitive cell-based infectivity assay for mouse scrapie prions. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 11666-11671
25. Kornblatt J.A., Marchal S., Rezaei H., Kornblatt M.J., Balny C., Lange R., Debey M.P., Hui B., Hoa G., Marden M.C., and Grosclaude J. The fate of the prion protein in the prion/plasminogen complex. Biochem. Biophys. Res. Commum. 305 (2003) 518-522
26. Kurt T.D., Perrott M.R., Wilusz C.J., Wilusz J., Supattapone S., Telling G.C., Zabel M.D., and Hoover E.A. Efficient in vitro amplification of chronic wasting disease PrPres. J. Virol. 81 (2007) 9605-9608
27. LaFauci G., Carp R.I., Meeker H.C., Ye X., Kim J.-I., Natelli M., Cedeno M., Petersen R.B., Kascsak R., and Rubenstein R. Passage of chronic wasting disease prion into transgenic mice expressing Rocky Mountain elk (Cervus elaphus nelsoni) PrPC. J. Gen. Virol. 87 (2006) 3773-3780
28. Lasmezas C.I., Deslys J.P., Robain O., Jaegly A., Beringue V., Peyrin J.M., Fournier J.G., Hauw J.J., Rossier J., and Dormont D. Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science 275 (1997) 402-405
29. Le Dur A., Beringue V., Andreoletti O., Reine F., Lai T.L., Baron T., Bratberg B., Vilotte J.L., Sarradin P., Benestad S.L., and Laude H. A newly identified type of scrapie agent can naturally infect sheep with resistant PrP genotypes. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 16031-16036
30. Litao Y., Fung C.W., Eun J.C., and Ellington A.D. Real-time rolling circle amplification for protein detection. Anal. Chem. 79 (2007) 3320-3329
31. Lourenco P.C., Schmerr M.J., MacGregor I., Will R.G., Ironside J.W., and Head M.W. Application of an immunocapillary electrophoresis assay to the detection of abnormal prion protein in brain, spleen and blood specimens from patients with variant Creutzfeldt-Jakob disease. J. Gen. Virol. 87 (2006) 3119-3124
32. Manuelidis L., Fritch W., and Xi Y.G. Evolution of a strain of CJD that induces BSE-like plaques. Science 277 (1997) 94-98
33. Murayama Y., Yoshioka M., Horii H., Takata M., Yokoyama T., Sudo T., Sato K., Shinagawa M., and Mohri S. Protein misfolding cyclic amplification as a rapid test for assessment of prion inactivation. Biochem. Biophys. Res. Commun. 348 (2006) 758-762
34. Negredo C., Monks E., and Sweeney T. A novel real-time ultrasonic method for prion protein detection using plasminogen as a capture molecule. BMC Biotechnol. 7 (2007) 43-49
35. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 13363-13383
36. Prusiner S.B. In: Prusiner S.B. (Ed). Prion Biology and Diseases (2004), Cold Spring Harbor Laboratory Press, New York
37. C by multi-spectral ultraviolet fluorescence. Biochem. Biophys. Res. Commun. 246 (1998) 100-106
38. Saa P., Castilla J., and Soto C. Presymptomatic detection of prions in blood. Science 313 (2006) 92-94
39. Saa P., Castilla J., and Soto C. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J. Biol. Chem. 281 (2006) 35245-35252
40. Saborio G.P., Permanne B., and Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411 (2001) 810-813
41. Safar J.G., Geschwind M.D., Deering C., Didorenko S., Sattavat M., Sanchez H., Serban A., Vey M., Baron H., Giles K., Miller B.L., DeArmond S.J., and Prusiner S.B. Diagnosis of human prion disease. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 3501-3506
42. Sc molecules with different conformations. Nat. Med. 4 (1998) 1157-1165
43. Schmerr M.J., Jenny A., and Cutlip R.C. Use of capillary sodium dodecyl sulfate gel electrophoresis to detect the prion protein extracted from scrapie-infected sheep. J. Chromatogr. A 697 (1997) 223-229
44. Schmerr M.J., Jenny A.L., Bulgin M.S., Miller J.M., Hamir A.N., Cutlip R.C., and Goodwin K.R. Use of capillary electrophoresis and fluorescent labeled peptides to detect the abnormal prion protein in the blood of animals that are infected with a transmissible spongiform encephalopathy. J. Chromatogr. B 853 (1999) 207-214
45. Schmitt J., Beekes M., Brauer A., Udelhoven T., Lasch P., and Naumann D. Identification of scrapie infection from blood serum by Fourier transform infrared spectroscopy. Anal. Chem. 74 (2002) 3865-3868
46. Silveira J.R., Raymond G.J., Hughson A.G., Race R.E., Sim V.L., Hayes S.F., and Caughey B. The most infectious prion protein particles. Nature 437 (2005) 257-261
47. Soto C. Diagnosing prion diseases: needs, challenges and hopes. Nat. Rev. Microbiol. 2 (2004) 809-819
48. Soto C., Anderes L., Suardi S., Cardone F., Castilla J., Frossard M.J., Peano S., Saa P., Limido L., Carbonatto M., Ironside J., Torres J.M., Pocchiari M., and Tagliavini F. Pre-symptomatic detection of prions by cyclic amplification of protein misfolding. FEBS Lett. 579 (2005) 638-642
49. Soto C., Saborio G.P., and Anderes L. Cyclic amplification of protein misfolding: application to prion-related disorders and beyond. Trends Neurosci. 25 (2002) 390-394
50. Thackray A.M., Hopkins L., and Bujdoso R. Proteinase K-sensitive disease-associated ovine prion protein revealed by conformation-dependent immunoassay. Biochem. J. 401 (2007) 475-483
51. Thackray A.M., Hopkins L., Klein M.A., and Bujdoso R. Mouse-adapted ovine scrapie prion strains are characterized by different conformers of PrPSc. J. Virol. 81 (2007) 12119-12127
52. Tremblay P., Ball H.L., Kaneko K., Groth D., Hegde R.S., Cohen F.E., DeArmond S.J., Prusiner S.B., and Safar J.G. Mutant PrPSc conformers induced by a synthetic peptide and several prion strains. J. Virol. 78 (2004) 2088-2099
53. Tzaban S., Friedlander G., Schonberger O., Horonchilk L., Yedidia Y., Shaked G., Gabizon R., and Taraboulos A. Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes. Biochemistry 41 (2002) 12868-12875
54. Yang W.C., Schmerr M.J., Jackman R., Bodemer W., and Yeung E.S. Capillary electrophoresis-based noncompetitive immunoassay for the prion protein using fluorescein-labeled protein A as a fluorescent probe. Anal. Chem. 77 (2005) 4489-4494