Nanopore detection of antibody prion interactions

Analytical Biochemistry

Volumn 396, Issue 1, 2010, Pages 36-41

  Madampage, Claudia Avis ^a   Andrievskaia, Olga ^b   Lee, Jeremy S ^a  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

^b CANADIAN FOOD INSPECTION AGENCY   (Canada)

Author keywords

Electrochemical detection; Monoclonal antibodies; Nanopore; Prions; Transmissible spongiform encephalopathy; Hemolysin

Indexed keywords

BLOOD; MOLECULES; MONOCLONAL ANTIBODIES; NANOPORES; NEURODEGENERATIVE DISEASES; PEPTIDES;

ELECTROCHEMICAL DETECTION; IMMUNOGLOBULIN G; LIPID MEMBRANES; PRION PROTEIN; PRIONS; SINGLE MOLECULE; TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES;

CHEMICAL DETECTION;

IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; PEPTIDE; PRION PROTEIN; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ANTIBODY SPECIFICITY; ANTIGEN BINDING; ARTICLE; CARBOXY TERMINAL SEQUENCE; NANOPORE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN INTERACTION;

EID: 70449639711     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.08.028     Document Type: Article

References (46)

1. Prusiner S.B. Neurodegenerative diseases and prions. N. Engl. J. Med. 344 (2001) 1516-1526
2. Cobb N.J., and Surewicz W.K. Prion diseases and their biochemical mechanisms. Biochemistry 48 (2009) 2574-2585
3. Collinge J., and Clarke A.R. A general model of prion strains and their pathogenicity. Science 318 (2007) 930-936
4. Chien P., Weissman J.S., and DePace A.H. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 73 (2004) 617-656
5. Bennion B.J., DeMarco M.L., and Daggett V. Preventing misfolding of the prion protein by trimethylamine N-oxide. Biochemistry 43 (2004) 12955-12963
6. Morillas M., Vanik D.L., and Surewicz W.K. On the mechanism of α-helix to β-sheet transition in the recombinant prion protein. Biochemistry 40 (2001) 6982-6987
7. 2 concept. Annu. Rev. Biophys. 37 (2008) 215-246
8. Chiti F., and Dobson C.F. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
9. Gaggelli E., Kozlowski H., Valensin D., and Valensin G. Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis). Chem. Rev. 106 (2006) 1995-2044
10. Lansbury P.T., and Lashuel H.A. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443 (2006) 774-779
11. 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
12. Sc replication in vitro generates unique infectious prions. Cell 134 (2008) 757-768
13. Seeger H., Heikenwalder M., Zeller N., Kranich J., Schwarz P., Gaspert A., Seifert B., Miele G., and Aguzzi A. Coincident scrapie infection and nephritis lead to urinary prion excretion. Science 310 (2005) 324-326
14. Sage L. Detecting prions in blood. Anal. Chem. 78 (2006) 14
15. Sc in mammary glands of sheep affected by scrapie and mastitis. Nat. Med. 11 (2005) 1137-1138
16. Soto C. Diagnosing prion diseases: needs, challenges, and hopes. Nat. Rev. Microbiol. 2 (2004) 809-819
17. Hill A.F., Zeidler M., Eronsid J., and Collinge J. Diagnosis of new variant Creutzfeldt-Jakob disease by tonsil biopsy. Lancet 349 (1997) 99-100
18. Caughey B., and Baron G.S. Prions and their partners in crime. Nature 443 (2006) 803-810
19. Paramithiotis E., Pinard M., Lawton T., Laboissier S., Leathers V.L., Zou W., Estey L.A., Lamontagne J., Lehto M.T., Kondejewski L.H., Francoeur G.P., Papadopoulos M., Haghighat A., Spatz S.J., Head M., Will R., Ironside J., O'Rourke K., Tonelli Q., Ledebur H.C., Chakrabartty A., and Cashman N.R. A prion protein epitope selective for the pathologically misfolded conformation. Nat. Med. 9 (2003) 893-899
20. Caughey B. Probing for prions: recognizing misfolded PrP. Nat. Med. 9 (2003) 819-820
21. Groschup M.H., Harmeyer S., and Pfaff E. Antigenic features of prion proteins of sheep and of other mammalian species. J. Immunol. Methods 207 (1997) 89-101
22. Demart S., Fournier J.G., Creminon C., Frobert Y., Lamoury F., Marce D., Lasmézas C., Dormont D., Grassi J., and Deslys J.P. New insight into abnormal prion protein using monoclonal antibodies. Biochem. Biophys. Res. Commun. 265 (1999) 652-657
23. Kascsak R.J., Fersko R., Pugiano D., Rubenstein R., and Carp R.I. Immunodiagnosis of prion disease. Immunol. Invest. 26 (1997) 259-268
24. Sc)-specific epitope defined by a monoclonal antibody. Nature 390 (1997) 74-77
25. Čurin Šerbec V., Bresjanac M., Popović M., Pretnar Hartman K., Galvani V., Rupreht R., Černilec M., Vranac T., Hafner I., and Jerala R. Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeld-Jacob's disease-affected and normal brain tissue. J. Biol. Chem. 279 (2004) 3694-3698
26. Zou W.Q., Zheng J., Gray D.M., Gambetti P., and Chen S.G. Antibody to DNA detects scrapie but not normal prion protein. Proc. Natl. Acad. Sci. USA 101 (2004) 1380-1385
27. Andrievskaia O., McRae H., Elmgren C., Huang H., Balachandran A., and Nielsen K. Generation of antibodies against bovine recombinant prion protein in various strains of mice. Clin. Vaccine Immunol. 13 (2006) 98-105
28. Polymenidou M., Moos R., Scott M., Sigurdson C., Shi Y., Yajima B., Hafner-Bratkovi I., Jerala R., Hornemann S., Wuthrich K., Bellon A., Vey M., Garen G., James M.N.G., Kav N., and Aguzzi A. The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes. PLoS One 3 (2008) e3872
29. Antonyuk S.V., Trevitt C.R., Strange R.W., Jackson G.S., Sangar D., Batchelor M., Cooper S., Fraser C., Jones S., Georgiou T., Khalili-Shirazi A., Clarke A.R., Hasnain S.S., and Collinge J. Crystal structure of human prion protein bound to a therapeutic antibody. Proc. Natl. Acad. Sci. USA 106 (2009) 2554-2558
30. Heppner F.L., Musahl C., Arrighi I., Klein M.A., Rülicke T., Oesch B., Zinkernagel R.M., Kalinke U., and Aguzzi A. Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies. Science 294 (2001) 178-182
31. Sutherland T.C., Long Y., Stefureac R., Bediako-Amoa I., Kraatz H., and Lee J.S. Structure of peptides investigated by nanopore analysis. Nano Lett. 4 (2004) 1273-1277
32. Movileanu L., Schmittschmitt J.P., Scholtz J.M., and Bayley H. Interactions of peptides with a protein pore. Biophys. J. 89 (2005) 1030-1045
33. Mohammad M.M., and Movileanu L. Excursion of a single polypeptide into a protein pore: simple physics, but complicated biology. Eur. Biophys. J. 37 (2008) 913-925
34. Zhao Q., Jayawardhana D.A., Wang D., and Guan X. Study of peptide transport through engineered protein channels. J. Phys. Chem. B 113 (2009) 3572-3578
35. Movileanu L. Squeezing a single polypeptide through a nanopore. Soft Matter 4 (2008) 925-931
36. Movileanu L. Interrogating single proteins through nanopores: challenges and opportunities. Trends Biotechnol. 27 (2006) 333-341
37. Wolfe A.J., Mohammad M.M., Cheley S., Bayley H., and Movileanu L. Catalyzing the translocation of polypeptides through attractive interactions. J. Am. Chem. Soc. 129 (2007) 14034-14041
38. Stefureac R., Long Y., Kraatz H., Howard P., and Lee J.S. Transport of α-helical peptides through α-hemolysin and aerolysin pores. Biochemistry 45 (2006) 9172-9179
39. Goodrich C.P., Kirmizialtin C., Huyghues-Despointes B.M., Zhu A., Scholtz J., Makarov D.E., and Movileanu L. Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. J. Phys. Chem. B 111 (2007) 3332-3335
40. Stefureac R., and Lee J.S. Nanopore analysis of the folding of zinc fingers. Small 4 (2008) 1646-1650
41. Dekker C. Solid-state nanopores. Nat. Nanotechnol. 2 (2007) 209-215
42. Siwy Z., Trofin L., Kohli P., Baker L.A., Trautmann C., and Martin C.R. Protein biosensors based on biofunctionalized conical gold nanotubes. J. Am. Chem. Soc. 127 (2005) 5000-5001
43. Hurt N., Wang H., Akeson M., and Lieberman K.R. Specific nucleotide binding and rebinding to individual DNA polymerase complexes captured on a nanopore. J. Am. Chem. Soc. 131 (2009) 3772-3778
44. Han N., Creus M., Schurmann G., Linder V., Ward T.R., de Roos N.F., and Staufer U. Label-free detection of single protein molecules and protein-protein interactions using synthetic nanopores. Anal. Chem. 80 (2008) 4651-4658
45. Oukhaled G., Mathé J., Biance A.L., Bacri L., Betton J.M., Lairez D., Pelta J., and Auvray L. Unfolding of proteins and long transient conformations detected by single nanopore recording. Phys. Rev. Lett. 98 (2007) 158101-158104
46. Stefureac R., Waldner L., Howard P., and Lee J.S. Nanopore analysis of a small 86-residue protein. Small 4 (2008) 59-63