Synthesis of high avidity antibody fragments (scFv multimers) for cancer imaging

Journal of Immunological Methods

Volumn 242, Issue 1-2, 2000, Pages 193-204

  Power, Barbara E ^a   Hudson, Peter J ^a,b  

^a CSIRO   (Australia)

^b CRC for Diagnostics   (Australia)

Author keywords

Antibody; E. coli; Heat induction; Multimers; scFv; Soluble

Indexed keywords

ANTIBODY; BACTERIAL PROTEIN; IMMUNOGLOBULIN FRAGMENT; IMMUNOGLOBULIN HEAVY CHAIN; POLYMER;

ANTIBODY PRODUCTION; ARTICLE; ESCHERICHIA COLI; EXPRESSION VECTOR; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PURIFICATION; TUMOR LOCALIZATION;

AMINO ACID SEQUENCE; ANTIBODIES, NEOPLASM; ANTIBODY AFFINITY; BASE SEQUENCE; DIAGNOSTIC IMAGING; HUMAN; IMMUNOGLOBULIN FRAGMENTS; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR SEQUENCE DATA; NEOPLASMS; TEMPERATURE;

EID: 0034726409     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(00)00201-5     Document Type: Article

References (33)

1. Adams G.P., Schier R., McCall A.M., Crawford R.S., Wolf E.J., Weiner L.M., Marks J.D. Prolonged in vivo tumor retention of a human diabody targeting the extracellular domain of human HERk2/neu. Br. J. Cancer. 77:1998;1405.
2. Arndt K.M., Muller K.M., Plückthun A. Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment. Biochemistry. 37:1998;12918.
3. L domains dictates precisely the transition between diabodies and triabodies. Protein Eng. 12:1999;101.
4. Atwell J.L., Pearce L.A., Lah M., Gruen L.C., Kortt A.A., Hudson P.J. Design and expression of a stable bispecific scFv dimer with affinity for both glycophorin and N9 neuraminidase. Molec. Immunol. 33:1996;1301.
5. Coia G., Hudson P.J., Lilley G.G. Construction of recombinant extended single-chain antibody peptide conjugates for use in the diagnosis of HIV1 and HIV2. J. Immunol. Methods. 192:1996;13.
6. Colcher D., Pavlinkova G., Beresford G., Booth B.J.M., Choudhury A., Batra S.K. Pharmacokinetics and biodistribution of genetically-engineered antibodies. Quart. J. Nucl. Med. 42:1998;225.
7. Dower W.J. Electroporation of bacteria: a general approach to genetic transformation. Genet. Eng. NY. 12:1990;275.
8. Harlow E., Lane D. Antibodies - A laboratory manual. 1988;Cold Spring Harbor Laboratory, Cold Spring Habor.
9. Ernst J.F. Codon usage and gene expression. TibTech. 6:1988;196.
10. FitzGerald K., Holliger P., Winter G. Improved tumor targeting by disulphide stabilized diabodies expressed in Pichia pastoris. Protein. Eng. 10:1997;1221.
11. Holliger P., Prospero T., Winter G. 'Diabodies': small bivalent and bispecific antibody fragments. Proc. Natl. Acad. Sci. USA. 90:1993;6444.
12. Hudson P.J. Recombinant antibody constructs in cancer therapy. Curr. Opin. Immunol. 11:(5):1999;548.
13. Hudson P.J., Kortt A.A. High avidity ScFv multimers; diabodies and triabodies. J. Immunol. Meth. 231:1999;177.
14. Iliades P., Kortt A.A., Hudson P.J. Triabodies: single chain Fv fragments without a linker form trivalent trimers. Febs. Lett. 409:1997;437.
15. Kabat E.A., Wu T.T., Perry H.M., Gottensman K.S., Foeller C. Sequences of Proteins of Immunological Interest. 1991;US Department of Health and Human Service, US Public Health service, NIH, Bethesda, MD.
16. Kipriyanov S.M., Moldenhauer G., Little M. High level production of soluble single chain antibodies in small-scale Escherichia coli cultures. J. Immunol. Methods. 200:1997;69.
17. Kortt A., Malby R., Caldwell J., Gruen L., Ivancic N., Lawrence M., Howlett G., Webster R., Hudson P., Colman P. Recombinant anti-neuraminidase single chain Fv antibody: characterization, formation of dimer and higher molecular mass multimers and the solution of the crystal structure of the scFv-neuraminidase complex. Eur. J. Biochem. 221:1994;151.
18. H domain of anti-neuraminidase antibody NC41. J. Protein Chem. 14:1995;167.
19. Kortt A.A., Lah M., Oddie G.W., Gruen L.C., Burns J.E., Pearce L.A., Atwell J.A., McCoy A.J., Howlett G.J., Metzger D.W., Webster R.G., Hudson P.J. Single chain Fv fragments of anti-neuraminidase antibody NC10 containing five and ten residue linkers form dimers and with zero residue linker a trimer. Protein Eng. 10:1997;423.
20. Lawrence L.J., Kortt A.A., Iliades P., Tulloch P.A., Hudson P.J. Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments. FEBS Lett. 425:1998;479.
21. Le Gall F., Kipriyanov S.M., Moldenhauer G., Little M. Di-, tri- and tetrameric single chain Fv antibody fragments against human CD19: effect of valency on cell binding. FEBS Lett. 453:1999;164.
22. Malby R., Caldwell J., Gruen L., Harley V., Ivancic N., Kortt A., Lilley G., Power B., Webster R., Colman P., Hudson P. Recombinant anti-neuraminidase single chain antibody: expression, characterisation and crystallisation in complex with antigen. Proteins: Structure, Function Genet. 16:1993;57.
23. Malby R.L., McCoy A.J., Kortt A.A., Hudson P.J., Colman P.M. Single-chain fv/neuraminidase complexes: Different stoichiometry in solution and crystals. J. Mol. Biol. 279:1998;901.
24. Muller K.M., Arndt K.M., Plückthun A. Model and simulation of multivalent binding to fixed ligands. Anal. Biochem. 261:1998;149.
25. Nieba L., Honegger A., Krebber C., Plückthun A. Disrupting the hydrophobic patches at the antibody variable/constant domain interphase: improved in vivo folding and physical characterisation of an engineered scFv fragment. Protein Eng. 10:(4):1997;435.
26. Owens R.J., Young R.J. The genetic engineering of monoclonal antibodies. J. Immunol. Methods. 168:1994;149.
27. Plückthun A., Pack P. New protein engineering approaches to multivalent and bispecific antibody fragments. Immunotechnology. 3:1997;83.
28. H -domain in Escherichia coli using the PelB secretion signal. Gene. 113:1992;95.
29. Schmidt T.G., Skerra A. One-step affinity purification of bacterially produced proteins by means of the 'Strep tag' and immobilised recombinant core streptavidin. J. Chromatogr. A. 676:(2):1994;337.
30. Skerra A. Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli. Gene. 151:(1-2):1994;131.
31. Wu A.M., Chen W., Raubitschek A., Williams L.E., Neumaier M., Fischer R., Hu S.-Z., Odom-Maryon T., Wong J.Y.C., Shively J.E. Tumor localisation of anti-CEA single chain Fvs: improved targeting by non-covalent dimers. Immunotechnology. 2:1996;21.
32. Wu A.M., Williams L.E., Zieran L., Padma A., Sherman M., Bebb G.G., Odom-Maryon T., Wong J.Y.C., Shively J.E., Raubitschek A.A. Anti-carcinoembryonic antigen (CEA) diabody for rapid tumor targeting and imaging. Tumor Targeting. 4:1999;47.
33. Zhu Z., Zapata G., Shalaby R., Snedecor B., Chen H., Carter P. High level secretion of a humanised bispecific diabody from E. coli. Nature Biotechnol. 14:1996;192.