Modulation of Alzheimer's β-amyloid neurotoxicity by site-directed single-chain antibody

Journal of Neuroimmunology

Volumn 106, Issue 1-2, 2000, Pages 23-31

  Frenkel, Dan ^a   Solomon, Beka ^a   Benhar, Itai ^a  

^a TEL AVIV UNIVERSITY   (Israel)

Author keywords

Amyloid modulation; Engineered antibodies; Neurotoxicity

Indexed keywords

AMYLOID BETA PROTEIN; RECOMBINANT ANTIBODY;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ANTIBODY AFFINITY; ARTICLE; IMMUNOGLOBULIN VARIABLE REGION; IMMUNOMODULATION; NEUROTOXICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN STABILITY;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; ANIMALS; ANTIBODIES; CLONING, MOLECULAR; HUMANS; HYBRIDOMAS; IMMUNOGLOBULIN FRAGMENTS; IMMUNOGLOBULIN M; IMMUNOGLOBULIN VARIABLE REGION; MUTAGENESIS, SITE-DIRECTED; NEUROTOXINS; PC12 CELLS; PEPTIDE FRAGMENTS; RATS;

EID: 0034237142     PISSN: 01655728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-5728(99)00232-5     Document Type: Article

References (39)

1. Anavi S. Locking the N-terminal of the Alzheimer β-amyloid Peptide Prevents the Neurotoxicity in Cell Cultures. 1998;. M.Sc. Thesis.
2. Ashall F., Goate A.M. Role of the β-amyloid precursor protein in Alzheimer's disease. Trends. Biochem. Sci. 19:1994;42-46.
3. Barrow J.C., Yasuda A., Kenny M.T.P., Zagorski G.M. Solution conformation and aggregation properties of synthetic amyloid β-peptides of Alzheimer's disease. J. Mol. Biol. 225:1992;1075-1093.
4. Berdichevsky Y., Lamed R., Frenkel D., Gophna U., Bayer E., Yaron S., Shoham Y., Benhar I. Matrix-assisted refolding of single-chain Fv-cellulose binding domain fusion proteins. Protein expression and purification. 17:1999;249-259.
5. Berdichevsky Y., Ben-Zeev E., Lamed R., Benhar I. Phage display of a cellulose binding domain from Clostridium thermocellum and its application as a tool for antibody engineering. J. Immunol. Methods. 228:1999;151-162.
6. Brightman M.W., Ishihara S., Chang L. Penetration of solutes, viruses and cells across the blood brain barrier. Curr. Top. Microbiol. Immunol. 202:1995;63-78.
7. Chothia C., Lesk A.M., Tramontano A., Levitt M., Smith-Gill S.J., Air G., Sheriff S., Padlan E.A., Davies D., Tulip W.R., Colman M.P., Spinelli S., Alzari M.P., Poljak J.R. Conformations of immunoglobulin hypervariable regions. Nature. 342:1989;877-883.
8. Cruz L., Urbanc B., Buldyrev S.V., Christie R., Gomez-Isla T., Havlin S., McNamara M., Stanley H.E., Hyman B.T. Aggregation and disaggregation of senile plaques in Alzheimer's disease. Proc. Natl. Acad. Sci. USA. 94:1997;7612-7616.
9. Frenkel D., Balass M., Katchalski-Katzir E., Solomon B. High affinity binding of monoclonal antibodies to the sequential epitope EFRH of beta-amyloid peptide is essential for modulation of fibrillar aggregation. J. Neuroimmunol. 95:1999;136-142.
10. Frenkel D., Balass M., Solomon B. N-terminal EFRH sequence of Alzheimer's β-amyloid peptide represents the epitope of its anti-aggregation antibodies. J. Neuroimmunol. 88:1998;85-90.
11. Golde T.E. Production of amyloid β protein from normal and mutated amyloid β protein precursors. Masters C.L., Beyreuther K., Trillet M., Christen Y. Amyloid Protein Precursor in Development Aging and Alzheimer's Disease. 1994;36-45.
12. Hoogenboom H.R. Designing and optimizing library selection strategies for generating high affinity antibodies. Trends Biotechnol. 15:1997;62-70.
13. Hoogenboom H.R., de Bruine A.P., Hufton S.E., Hoet R.M., Arends J.W., Roovers R.C. Antibody phage display technology and its applications. Immunotechnology. 4:1998;1-20.
14. Kabat E.A., Wu T.T., Perry M.H., Gottesman S.K., Foeller C. 5th Edition Sequences of Proteins of Immunological Interest. 1991.
15. Kipriyanov M.S. Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on the bacterial secretion but not the affinity. Protein Eng. 10:1997;445-453.
16. Kirshenbaum K., Daggett V. Sequence effects on the conformational properties of the amyloid β(1-28) peptide: testing a proposed mechanism for the α→β transition. Biochemistry. 34:1995;7640-7647.
17. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;263-270.
18. Larocca D., Witte A., Johnson W., Pierce F.G., Baird A. Targeting bacteriophage to mammalian cell surface receptors for gene delivery. Human Gene Ther. 9:1998;2393-2399.
19. Lee J.P., Stimson E.R., Ghilardi J.R., Mantyh P.W., Lu Y-A., Felix A.F., Lianos W., Behbin A., Cummings M., Van Criekinge M., Timms W., Maggio J.E. HNMR of Aβ amyloid peptide congeners in water solution - conformational changes correlate with plaque competence. Biochemistry. 34:1995;5191-5200.
20. Lefebvre B., Formstecher P., Lefebvre P. Improvement of the gene splicing overlap (SOE) method. Biotechniques. 19:1995;186-188.
21. Levine H. III. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2:1993;404-410.
22. Lorenzo A., Yankner B.A. β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA. 91:1994;12243-12247.
23. Ma J., Brewer H.B. Jr., Potter H. Alzheimer A beta neurotoxicity: promotion by antichymotrypsin, ApoE4; inhibition by A beta-related peptides. Neurobiol. Aging. 17:1996;773-780.
24. McCafferty J., Griffith A.D., Winter G., Chiswell D.J. Phage antibodies: filamentous phage displaying antibody variable domains. Nature. 348:1990;552-554.
25. Morag E., Lapidot A., Govorko D., Lamed R., Wilchek M., Bayer E.A., Shoham Y. Expression, purification and characterization of the cellulose-binding domain of the scaffolding subunit from the cellulosome of Clostridium thermocellum. Appl. Environ. Microbiol. 61:1995;1980-1986.
26. Reiter Y., Brinkmann U., Jung S.H., Lee B., Kasprzyk P.G., King C.R., Pastan I. Improved binding and anti-tumor activity of a recombinant anti-erbB2 immunotoxin by disulfide stabilization of the Fv fragment. J. Biol. Chem. 269:1994;18327-18331.
27. Richardson H.J., Marasco A.W. Intracellular antibodies: development and therapeutic potential. Trends Biotechnol. 13:1995;306-310.
28. Rondon J.I., Marasco A.W. Intracellular antibodies (intrabodies) for gene therapy of infectious diseases. Annu. Rev. Microbiol. 51:1997;257-283.
29. Sambrook J.L., Fritsch E.F., Maniatis T. 2nd Edition Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
30. Skerra A., Pfitzinger I., Plückthun A. The functional expression of antibody Fv fragments in Escherichia coli: improved vectors and a generally applicable purification technique. Biotechnology (NY). 9:1991;273-278.
31. Sladowski D., Steer S.J., Clothier R.H., Balls M. An improved MTT assay. J. Immunol. Methods. 157:1993;203-207.
32. Solomon B., Koppel R., Frenkel D., Hanan-Aharon E. Disaggregation of Alzheimer β-amyloid by site-directed mAb. Proc. Natl. Acad. Sci. USA. 94:1997;4109-4112.
33. Solomon B., Koppel R., Hanan E., Katzav T. Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer β-amyloid peptide. Proc. Natl. Acad. Sci. USA. 93:1996;452-455.
34. Soto C., Castano E.M., Frangione B., Inestrosa N.C. The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation. J. Biol. Chem. 270:1995;3063-3067.
35. Studier F.W., Rosenberg A.H., Dunn J.J., Dubendorff J.W. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 85:1990;60-89.
36. Talafous J., Marcinowski K.J., Klopman G., Zagorski G.M. Solution structure of residues 1-28 of the amyloid β-peptide. Biochemistry. 33:1994;7788-7796.
37. Vines G. Alzheimer's disease - from cause to cure? Trends Biotechnol. 11:1993;49-55.
38. Winter G., Griffiths A.D., Hawkins R.E., Hoogenboom H.R. Making antibody by phage display technology. Annu. Rev. Immunol. 12:1994;433-455.
39. Zolkovic B. Can blood-brain barrier play a role in the development of cerebral amyloidosis and Alzheimer's disease pathology? Neurobiol. Dis. 4:1997;23-26.