DNA aptamers that bind to PrPC and not PrPSc show sequence and structure specificity

Experimental Biology and Medicine

Volumn 231, Issue 2, 2006, Pages 204-214

  Takemura, Kaori ^a   Wang, Ping ^a   Vorberg, Ina ^b   Surewicz, Witold ^c   Priola, Suzette A ^b   Kanthasamy, Anumantha ^c   Pottathil, Ravi ^d   Chen, Shu G ^e   Sreevatsan, Srinand ^a,f  

^a OHIO STATE UNIVERSITY   (United States)

^b NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^c IOWA STATE UNIVERSITY   (United States)

^d AccuDx Inc   (United States)

^e CASE WESTERN RESERVE UNIVERSITY   (United States)

^f UNIVERSITY OF MINNESOTA   (United States)

Author keywords

DNA aptamers; Prion; Scrapie; TSE

Indexed keywords

APTAMER; DNA; NUCLEIC ACID; NUCLEOTIDE; PRION PROTEIN; PROTEINASE K; RECOMBINANT PROTEIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BINDING SITE; CATTLE; CONCENTRATION (PARAMETERS); DNA BINDING; DNA SEQUENCE; EVALUATION; MAMMAL; MOLECULE; MOUSE; NEUROBLASTOMA CELL; NONHUMAN; NULL CELL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN MOTIF; SHEEP; SWINE; THEORY; THERMODYNAMICS;

ANIMALIA; BOS TAURUS; CERVIDAE; MAMMALIA; OVIS ARIES; SUS SCROFA;

EID: 32244440049     PISSN: 15353702     EISSN: 15353699     Source Type: Journal    
DOI: 10.1177/153537020623100211     Document Type: Article

References (35)

1. Prusiner SB. Prions. Proc Natl Acad Sci U S A 95:13363-13383, 1998.
2. Lasmezas CI, Deslys JP, Demaimay R, Adjou KT, Lamoury F, Dormont D, Robain O, Ironside J, Hauw JJ. BSE transmission to macaques. Nature 381:743-744, 1996.
3. Korth C, Stierli B, Streit P, Moser M, Schaller O, Fischer R, Schulz-Schaeffer W, Kretzschmar H, Raeber A, Braun U, Ehrensperger F, Hornemann S, Glockshuber R, Riek R, Billeter M, Wuthrich K, Oesch B. Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature 390:74-77, 1997.
4. Safar JG, Scott M, Monaghan J, Deering C, Didorenko S, Vergara J, Ball H, Legname G, Leclerc E, Solforosi L, Serban H, Groth D, Burton DR, Prusiner SB, Williamson RA. Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice. Nat Biotechnol 20:1147-1150, 2002.
5. Paramithiotis E, Pinard M, Lawton T, LaBoissiere S, Leathers VL, Zou WQ, Estey LA, Lamontagne J, Lehto MT, Kondejewski LH, Francoeur GP, Papadopoulos M, Haghighat A, Spatz SJ, Head M, Will R, Ironside J, O'Rourke K, Tonelli Q, Ledebur HC, Chakrabartty A, Cashman NR. A prion protein epitope selective for the pathologically misfolded conformation. Nat Med 9:893-899, 2003.
6. Tuerk C, Gold L. Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science 249:505-510, 1990.
7. Osborne SE, Ellington AD. Nucleic acid selection and the challenge of combinatorial chemistry. Chem Rev 97:349-370, 1997.
8. Clark SL, Remcho VT. Aptamers as analytical reagents. Electrophoresis 23:1335-1340, 2002.
9. Brody EN, Gold L. Aptamers as therapeutic and diagnostic agents. J Biotechnol 74:5-13, 2000.
10. Tavitian B. In vivo imaging with oligonucleotides for diagnosis and drug development. Gut 52(Suppl 4):iv40-47, 2003.
11. Patel DJ, Suri AK. Structure, recognition and discrimination in RNA aptamer complexes with cofactors, amino acids, drugs and aminoglycoside antibiotics. J Biotechnol 74:39-60, 2000.
12. Brody EN, Willis MC, Smith JD, Jayasena S, Zichi D, Gold L. The use of aptamers in large arrays for molecular diagnostics. Mol Diagn 4:381-388, 1999.
13. Weiss S, Proske D, Neumann M, Groschup MH, Kretzschmar HA, Famulok M, Winnacker EL. RNA aptamers specifically interact with the prion protein PrP. J Virol 71:8790-8797, 1997.
14. Proske D, Gilch S, Wopfner F, Schatzl HM, Winnacker EL, Famulok M. Prion-protein-specific aptamer reduces PrPSc formation. Chembiochem 3:717-725, 2002.
15. Zeiler B, Adler V, Kryukov V, Grossman A. Concentration and removal of prion proteins from biological solutions. Biotechnol Appl Biochem 37:173-182, 2003.
16. Sayer NM, Cubin M, Rhie A, Bullock M, Tahiri-Alaoui A, James W. Structural determinants of conformationally selective, prion-binding aptamers. J Biol Chem 279:13102-13109, 2004.
17. Zuker M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31:3406-3415, 2003.
18. SantaLucia J Jr. A unified view of polymer, dumbbell, and oligonucleotide DNA nearest-neighbor thermodynamics. Proc Natl Acad Sci U S A 95:1460-1465, 1998.
19. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685, 1970.
20. Priola SA, Chabry J, Chan K. Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155. J Virol 75:4673-4680, 2001.
21. Bosque PJ, Prusiner SB. Cultured cell sublines highly susceptible to prion infection. J Virol 74:4377-4386, 2000.
22. Otto M, Wiltfang J, Cepek L, Neumann M, Mollenhauer B, Steinacker P, Ciesielczyk B, Schulz-Schaeffer W, Kretzschmar HA, Poser S. Tau protein and 14-3-3 protein in the differential diagnosis of Creutzfeldt-Jakob disease. Neurology 58:192-197, 2002.
23. Gajdusek DC. Spontaneous generation of infectious nucleating amyloids in the transmissible and nontransmissible cerebral amyloidoses. Mol Neurobiol 8:1-13, 1994.
24. Alper T, Cramp WA, Haig DA, Clarke MC. Does the agent of scrapie replicate without nucleic acid? Nature 214:764-766, 1967.
25. Alper T. Scrapie agent unlike viruses in size and susceptibility to inactivation by ionizing or ultraviolet radiation. Nature 317:750, 1985.
26. Alper T. New insight into the nature of scrapie from old radiation results. BJR Suppl 24:1-5, 1992.
27. Collinge J, Sidle KC, Meads J, Ironside J, Hill AF. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383:685-690, 1996.
28. Collinge J, Beck J, Campbell T, Estibeiro K, Will RG. Prion protein gene analysis in new variant cases of Creutzfeldt-Jakob disease. Lancet 348:56, 1996.
29. Hill AF, Desbruslais M, Joiner S, Sidle KC, Gowland I, Collinge J, Doey LJ, Lantos P. The same prion strain causes vCJD and BSE. Nature 389:448-450, 526, 1997.
30. Hill AF, Will RG, Ironside J, Collinge J. Type of prion protein in UK farmers with Creutzfeldt-Jakob disease. Lancet 350:188, 1997.
31. MacGregor I. Prion protein and developments in its detection. Transfus Med 11:3-14, 2001.
32. Kretzschmar HA, Stowring LE, Westaway D, Stubblebine WH, Prusiner SB, Dearmond SJ. Molecular cloning of a human prion protein cDNA. DNA 5:315-324, 1986.
33. Riek R, Hornemann S, Wider G, Glockshuber R, Wuthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett 413:282-288, 1997.
34. Lyamichev V, Brow MA, Dahlberg JE. Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases. Science 260:778-783, 1993.
35. Barnes WM. PCR amplification of up to 35-kb DNA with high fidelity and high yield from lambda bacteriophage templates. Proc Natl Acad Sci U S A 91:2216-2220, 1994.