Kinetic screening of antibody-Im7 conjugates by capture on a colicin E7 DNase domain using optical biosensors

Analytical Biochemistry

Volumn 385, Issue 2, 2009, Pages 346-357

  Hosse, Ralf J ^a   Tay, Leigh ^a   Hattarki, Meghan K ^a   Pontes Braz, Luisa ^a   Pearce, Lesley A ^a   Nuttall, Stewart D ^a   Dolezal, Olan ^a  

^a CSIRO   (Australia)

Author keywords

Antibody capture; Biacore; Colicin E7; Kinetic screening; ProteOn; SPR

Indexed keywords

BIOSENSORS; CLONING; ESCHERICHIA COLI; KINETICS; PHAGE DISPLAY; SURFACE PLASMON RESONANCE; THERMODYNAMICS;

ANTIBODY CAPTURE; BIACORE; COLICIN E7; DISPLAY TECHNOLOGIES; ENZYME LINKED IMMUNOSORBENT ASSAY; KINETICS AND THERMODYNAMICS; PROTEON; SINGLE-DOMAIN ANTIBODIES;

ANTIBODIES;

ANTIBODY; ANTIBODY CONJUGATE; ANTIGEN; COLICIN; COLICIN E7; DEOXYRIBONUCLEASE; HYBRID PROTEIN; IMMUNITY PROTEIN 7; LIGAND; NUCLEASE; PROTEIN; RECOMBINANT ANTIBODY IM7 CONJUGATE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIGEN BINDING; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; ESCHERICHIA COLI; KINETICS; NONHUMAN; OPTICAL BIOSENSOR; PRIORITY JOURNAL; PROTEIN DOMAIN; SCREENING;

CHONDRICHTHYES;

EID: 58149402096     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.11.026     Document Type: Article

References (52)

1. Fuh G. Synthetic antibodies as therapeutics. Expert Opin. Biol. Ther. 7 (2007) 73-87
2. Sidhu S.S., and Fellouse F.A. Synthetic therapeutic antibodies. Nat. Chem. Biol. 2 (2006) 682-688
3. Holliger P., and Hudson P.J. Engineered antibody fragments and the rise of single domains. Nat. Biotechnol. 23 (2005) 1126-1136
4. Hoogenboom H.R. Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 23 (2005) 1105-1116
5. Buckler D.R., Park A., Viswanathan M., Hoet R.M., and Ladner R.C. Screening isolates from antibody phage-display libraries. Drug Discov. Today 13 (2008) 318-324
6. Watkins J.D., Beuerlein G., Pecht G., McFadden P.R., Glaser S.M., and Huse W.D. Determination of the relative affinities of antibody fragments expressed in Escherichia coli by enzyme-linked immunosorbent assay. Anal. Biochem. 253 (1997) 37-45
7. Fellouse F.A., Esaki K., Birtalan S., Raptis D., Cancasci V.J., Koide A., Jhurani P., Vasser M., Wiesmann C., Kossiakoff A.A., Koide S., and Sidhu S.S. High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries. J. Mol. Biol. 373 (2007) 924-940
8. Papalia G.A., Baer M., Luehrsen K., Nordin H., Flynn P., and Myszka D.G. High-resolution characterization of antibody fragment/antigen interactions using Biacore T100. Anal. Biochem. 359 (2006) 112-119
9. Säfsten P., Klakamp S.L., Drake A.W., Karlsson R., and Myszka D.G. Screening antibody-antigen interactions in parallel using Biacore A100. Anal. Biochem. 353 (2006) 181-190
10. Leonard P., Safsten P., Hearty S., McDonnell B., Finlay W., and O'Kennedy R. High throughput ranking of recombinant avian scFv antibody fragments from crude lysates using the Biacore A100. J. Immunol. Methods 323 (2007) 172-179
11. Canziani G.A., Klakamp S., and Myszka D.G. Kinetic screening of antibodies from crude hybridoma samples using Biacore. Anal. Biochem. 325 (2004) 301-307
12. Wassaf D., Kuang G., Kopacz K., Wu Q.L., Nguyen Q., Toews M., Cosic J., Jacques J., Wiltshire S., Lambert J., Pazmany C.C., Hogan S., Ladner R.C., Nixon A.E., and Sexton D.J. High-throughput affinity ranking of antibodies using surface plasmon resonance microarrays. Anal. Biochem. 351 (2006) 241-253
13. Steukers M., Schaus J.M., van G.R., Hoyoux A., Richalet P., Sexton D.J., Nixon A.E., and Vanhove M. Rapid kinetic-based screening of human Fab fragments. J. Immunol. Methods 310 (2006) 126-135
14. Klonisch T., Panayotou G., Edwards P., Jackson A.M., Berger P., Delves P.J., Lund T., and Roitt I.M. Enhancement in antigen binding by a combination of synergy and antibody capture. Immunology 89 (1996) 165-171
15. Peluso P., Wilson D.S., Do D., Tran H., Venkatasubbaiah M., Quincy D., Heidecker B., Poindexter K., Tolani N., Phelan M., Witte K., Jung L.S., Wagner P., and Nock S. Optimizing antibody immobilization strategies for the construction of protein microarrays. Anal. Biochem. 312 (2003) 113-124
16. Bravman T., Bronner V., Lavie K., Notcovich A., Papalia G.A., and Myszka D.G. Exploring "one-shot" kinetics and small molecule analysis using the ProteOn XPR36 array biosensor. Anal. Biochem. 358 (2006) 281-288
17. Natsume T., Taoka M., Manki H., Kume S., Isobe T., and Mikoshiba K. Rapid analysis of protein interactions: On-chip micropurification of recombinant protein expressed in Esherichia coli. Proteomics 2 (2002) 1247-1253
18. Li Y.J., Bi L.J., Zhang X.E., Zhou Y.F., Zhang J.B., Chen Y.Y., Li W., and Zhang Z.P. Reversible immobilization of proteins with streptavidin affinity tags on a surface plasmon resonance biosensor chip. Anal. Bioanal. Chem. 386 (2006) 1321-1326
19. Schmidt T.G., and Skerra A. The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat. Protoc. 2 (2007) 1528-1535
20. Nieba L., Nieba-Axmann S.E., Persson A., Hamalainen M., Edebratt F., Hansson A., Lidholm J., Magnusson K., Karlsson A.F., and Pluckthun A. Biacore analysis of histidine-tagged proteins using a chelating NTA sensor chip. Anal. Biochem. 252 (1997) 217-228
21. Khan F., He M., and Taussig M.J. Double-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on Ni-nitrilotriacetic acid surfaces. Anal. Chem. 78 (2006) 3072-3079
22. Ko T.P., Liao C.C., Ku W.Y., Chak K.F., and Yuan H.S. The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein. Structure 7 (1999) 91-102
23. Wallis R., Moore G.R., James R., and Kleanthous C. Protein-protein interactions in colicin E9 DNase-immunity protein complexes: I. Diffusion-controlled association and femtomolar binding for the cognate complex. Biochemistry 34 (1995) 13743-13750
24. Wallis R., Leung K.Y., Pommer A.J., Videler H., Moore G.R., James R., and Kleanthous C. Protein-protein interactions in colicin E9 DNase-immunity protein complexes: II. Cognate and noncognate interactions that span the millimolar to femtomolar affinity range. Biochemistry 34 (1995) 13751-13759
25. Hsieh S.Y., Ko T.P., Tseng M.Y., Ku W., Chak K.F., and Yuan H.S. A novel role of ImmE7 in the autoregulatory expression of the ColE7 operon and identification of possible RNase active sites in the crystal structure of dimeric ImmE7. EMBO J. 16 (1997) 1444-1454
26. Cheng Y.S., Hsia K.C., Doudeva L.G., Chak K.F., and Yuan H.S. The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases. J. Mol. Biol. 324 (2002) 227-236
27. Cramer W.A., Lindeberg M., and Taylor R. The best offense is a good defense. Nat. Struct. Biol. 6 (1999) 295-297
28. Dolezal O., Pearce L.A., Lawrence L.J., McCoy A.J., Hudson P.J., and Kortt A.A. ScFv multimers of the anti-neuraminidase antibody NC10: Shortening of the linker in single-chain Fv fragment assembled in V(L) to V(H) orientation drives the formation of dimers, trimers, tetramers and higher molecular mass multimers. Protein Eng. 13 (2000) 565-574
29. Malby R.L., Caldwell J.B., Gruen L.C., Harley V.R., Ivancic N., Kortt A.A., Lilley G.G., Power B.E., Webster R.G., and Colman P.M. Recombinant antineuraminidase single chain antibody: Expression, characterization, and crystallization in complex with antigen. Proteins 16 (1993) 57-63
30. Juraja S.M., Mulhern T.D., Hudson P.J., Hattarki M.K., Carmichael J.A., and Nuttall S.D. Engineering of the Escherichia coli Im7 immunity protein as a loop display scaffold. Protein Eng. Des. Sel. 19 (2006) 231-244
31. 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., and Raubitschek A.A. Anti-carcinoembryonic antigen (CEA) diabody for rapid tumor targeting and imaging. Tumor Target. 4 (1999) 47-58
32. Nuttall S.D., Humberstone K.S., Krishnan U.V., Carmichael J.A., Doughty L., Hattarki M., Coley A.M., Casey J.L., Anders R.F., Foley M., Irving R.A., and Hudson P.J. Selection and affinity maturation of IgNAR variable domains targeting Plasmodium falciparum AMA1. Proteins 55 (2004) 187-197
33. Dertzbaugh M.T., Rossi C.A., Paddle B.M., Hale M., Poretski M., and Alderton M.R. Monoclonal antibodies to ricin: In vitro inhibition of toxicity and utility as diagnostic reagents. Hybridoma 24 (2005) 236-243
34. Gilliland L.K., Norris N.A., Marquardt H., Tsu T.T., Hayden M.S., Neubauer M.G., Yelton D.E., Mittler R.S., and Ledbetter J.A. Rapid and reliable cloning of antibody variable regions and generation of recombinant single chain antibody fragments. Tissue Antigens 47 (1996) 1-20
35. H) molecule is primarily responsible for formation of a tetramer-trimer equilibrium. Protein Eng. 16 (2003) 47-56
36. Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
37. Metzger D.W., and Webster R.G. In: Osterhaus A.D.M.E., and Uytdellaag F.G.C.M. (Eds). Idiotype Networks in Biology and Medicine (1990), Elsevier, Amsterdam 257-267
38. Simmons D.P., Streltsov V.A., Dolezal O., Hudson P.J., Coley A.M., Foley M., Proll D.F., and Nuttall S.D. Shark IgNAR antibody mimotopes target a murine immunoglobulin through extended CDR3 loop structures. Proteins 71 (2008) 119-130
39. Myszka D.G. Improving biosensor analysis. J. Mol. Recognit. 12 (1999) 279-284
40. Simmons D.P., Abregu F.A., Krishnan U.V., Proll D.F., Streltsov V.A., Doughty L., Hattarki M.K., and Nuttall S.D. Dimerisation strategies for shark IgNAR single domain antibody fragments. J. Immunol. Methods 315 (2006) 171-184
41. Kortt A.A., Malby R.L., Caldwell J.B., Gruen L.C., Ivancic N., Lawrence M.C., Howlett G.J., Webster R.G., Hudson P.J., and Colman P.M. Recombinant anti-sialidase single-chain variable fragment antibody: Characterization, formation of dimer and higher-molecular-mass multimers,and the solution of the crystal structure of the single-chain variable fragment/sialidase complex. Eur. J. Biochem. 221 (1994) 151-157
42. Muller K.M., Arndt K.M., and Pluckthun A. Model and simulation of multivalent binding to fixed ligands. Anal. Biochem. 261 (1998) 149-158
43. Kortt A.A., Dolezal O., Power B.E., and Hudson P.J. Dimeric and trimeric antibodies: High avidity scFvs for cancer targeting. Biomol. Eng. 18 (2001) 95-108
44. Wu A.M., Chen W., Raubitschek A., Williams L.E., Neumaier M., Fischer R., Hu S.Z., Odom-Maryon T., Wong J.Y., and Shively J.E. Tumor localization of anti-CEA single-chain Fvs: Improved targeting by non-covalent dimers. Immunotechnology 2 (1996) 21-36
45. Katsamba P.S., Navratilova I., Calderon-Cacia M., Fan L., Thornton K., Zhu M., Bos T.V., Forte C., Friend D., Laird-Offringa I., Tavares G., Whatley J., Shi E., Widom A., Lindquist K.C., Klakamp S., Drake A., Bohmann D., Roell M., Rose L., Dorocke J., Roth B., Luginbuhl B., and Myszka D.G. Kinetic analysis of a high-affinity antibody/antigen interaction performed by multiple Biacore users. Anal. Biochem. 352 (2006) 208-221
46. Tran H., Leong C., Loke W.K., Dogovski C., and Liu C.Q. Surface plasmon resonance detection of ricin and horticultural ricin variants in environmental samples. Toxicon 52 (2008) 582-588
47. Henderson K.A., Streltsov V.A., Coley A.M., Dolezal O., Hudson P.J., Batchelor A.H., Gupta A., Bai T., Murphy V.J., Anders R.F., Foley M., and Nuttall S.D. Structure of an IgNAR-AMA1 complex: Targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure 15 (2007) 1452-1466
48. Kopsidas G., Roberts A.S., Coia G., Streltsov V.A., and Nuttall S.D. In vitro improvement of a shark IgNAR antibody by Qβ replicase mutation and ribosome display mimics in vivo affinity maturation. Immunol. Lett. 107 (2006) 163-168
49. Green N.M. Avidin and streptavidin. Methods Enzymol. 184 (1990) 51-67
50. Hartley R.W. Barnase-barstar interaction. Methods Enzymol. 341 (2001) 599-611
51. Keefe A.D., Wilson D.S., Seelig B., and Szostak J.W. One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-tag. Protein Expr. Purif. 23 (2001) 440-446
52. Tudyka T., and Skerra A. Glutathione S -transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli. Protein Sci. 6 (1997) 2180-2187