Cooperative effects of mutations in a recombinant Fab on the kinetics of antigen binding

Molecular Immunology

Volumn 34, Issue 2, 1997, Pages 165-173

  Rauffer Bruyère, Nathalie ^a   Chatellier, Jean ^a,c   Weiss, Etienne ^b   Van Regenmortel, Marc H V ^a   Altschuh, Danièle ^a  

^a INSTITUT DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^b UNIVERSITÉ DE STRASBOURG   (France)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

antigen binding kinetics; BIAcore(TM); cooperativity; recombinant Fab; site directed mutagenesis; structure function relationship

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; GENE EXPRESSION; GENE LOCATION; GENE MUTATION; PHAGEMID; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; TOBACCO MOSAIC VIRUS;

ANTIGENS; BIOSENSING TECHNIQUES; GENETIC VECTORS; IMMUNOGLOBULIN FAB FRAGMENTS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; RESTRICTION MAPPING; STRUCTURE-ACTIVITY RELATIONSHIP;

NICOTIANA TABACUM; TOBACCO MOSAIC VIRUS;

EID: 0030904272     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0161-5890(97)00003-5     Document Type: Article

References (45)

1. Ackers G. K. and Smith F. R. (1985) Effetcs of site-directed amino acid modification on protein interactions and biological function. Ann. Rev. Biochem. 54, 597-629.
2. Barbas III C. F., HU D., Dunlop N., Sawyer L., Cababa D., Hendry R. M., Nara P. L. and Burton D. R. (1994) In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity. Proc. natn. Acad. Sci. U.S.A. 91, 3809-3813.
3. Blacklow S. C., Liu K. D. and Knowles J. R. (1991) Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase. Biochemistry 30, 8470-8476.
4. Carter P. J., Winter G., Wilkinson A. J. and Fersht A. R. (1984) The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell 38, 835-840.
5. Chatellier J., Van Regenmortel M. H. V., Vernet T. and Altschuh D. (1996a) Functional mapping of conserved residues located at the VL and VH domain interface of an Fab. J. Mol. Biol. 264, 1-6.
6. Chatellier J., Rauffer-Bruyère N., Van Regenmortel M. H. V., Altschuh D. and Weiss E. (1996b) Comparative interaction kinetics of two recombinant Fabs and of the corresponding antibodies directed to the coat protein of tobacco mosaic virus. J. Mol. Recog. 9, 39-51.
7. Chien N. C., Roberts V. A., Giusti A. M., Scharff M. D. and Getzoff E. D. (1989) Significant structural and functional change of an antigen-binding site by a distant amino acid substitution: proposal of a structural mechanism. Proc. natn. Acad. Sci. U.S.A. 86, 5532-5536.
8. Denzin L. K. and Voss E. W. Jr (1992) Construction, characterization, and mutagenesis of an anti-fluorescein single chain antibody idiotype family. J. Biol. Chem. 267, 8925-8931.
9. Felder S., Zhou M., Hu P., Urena J., Ullrich A., Chaudhuri M., White M., Shoelson S. E. and Schlessinger J. (1993) SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell. Biol. 13, 1449-1455.
10. Foote J. and Winter G. (1992) Antibody framework residues affecting the conformation of hypervariable loops. J. Mol. Biol. 224, 487-499.
11. Glaser R. W. (1993) Antigen-antibody binding and mass transport by convection and diffusion to a surface: a two-dimensional computer model of binding and dissociation kinetics. Anal. Biochem. 213, 152-161.
12. Green S. M. and Shortle D. (1993) Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. Biochemistry 32, 10131-10139.
13. Horovitz A. (1987) Non-additivity in protein-protein interactions. J. Mol. Biol. 196, 733-735.
14. Horovitz A. and Fersht A. R. (1990) Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins. J. Mol. Biol. 214, 613-617.
15. Howell E. E., Booth C., Farnum M., Kraut J. and Warren M. S. (1990) A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27 → serine Escherichia coli dihydrofolate reductase. Biochemistry 29, 8561-8569.
16. Jackson T., Morris B. A., Martin A. C., Lewis D. F. and Sanders P. G. (1992) Molecular modelling and site-directed mutagenesis on a bovine anti-testosterone monoclonal antibody. Prot. Eng. 5, 343-350.
17. Kelley R. F., Costas K. E., O'Connel M. P. and Lazarus R. A. (1995) Analysis of the factor VIIa binding site on human tissue factor: effects of tissue factor mutations on the kinetics and thermodynamics of binding. Biochemistry 34, 10383-10392.
18. Kettleborough C. A., Saldanha J., Heath V. J., Morrison C. J. and Bendig M. M. (1991) Humanization of a mouse monoclonal antibody by CDR-grafting: the importance of framework residues on loop conformation. Prot. Eng. 4, 773-783.
19. Kraulis P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
20. Kunkel T. A., Roberts J. and Zakour R. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Meth. Enzym. 154, 367-382.
21. Lavoie T. B., Drohan W. N. and Smith-Gill S. J. (1992) Experimental analysis by site-directed mutagenesis of somatic mutation effects on affinity and fine specificity in antibodies specific for lysozyme. J. Immun. 148, 503-513.
22. LiCata V. J., Speros P. C., Rovida E. and Ackers G. K. (1990) Direct and indirect pathways of functional coupling in human hemoglobin are revealed by quantitative low-temperature isoelectric focusing of mutant hybrids. Biochemistry 29, 9771-9783.
23. LiCata V. J. and Ackers G. K. (1995) Long-range, small magnitude nonadditivity of mutational effects in proteins. Biochemistry 34, 3133-3139.
24. Lowman H. B. and Wells J. A. (1993) Affinity maturation of human growth hormone by monovalent phage display. J. Mol. Biol. 234, 564-578.
25. Mace J. E., Wilk B. J. and Agard D. A. (1995) Functional linkage between the active site of alpha-lytic protease and distant regions of structure: scanning alanine mutagenesis of a surface loop affects activity and substrate specificity. J. Mol. Biol. 251, 116-134.
26. O'Shannessy D. J., Brigham-Burke M., Soneson K. K., Hensley P. and Brooks I. (1993) Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods. Anal. Biochem. 212, 457-468.
27. Roberts S., Cheetham J. C. and Rees A. R. (1987) Generation of an antibody with enanced affinity and specificity for its antigen by protein engineering. Nature 328, 731-734.
28. Ruff-Jamison S. and Glenney J. R. Jr (1993) Molecular modeling and site-directed mutagenesis of an anti-phosphotyrosine antibody predicts the combining site and allows the detection of higher affinity interactions. Prot. Eng. 6, 661-668
29. Sambrook J., Fritsch E. F. and Maniatis T. (1989) Molecular Cloning: A Laboratory Manual, Second Edn. Cold Spring Harbor Laboratory Press. Cold Spring Harbor.
30. Sandberg W. S. and Terwilliger T. C. (1991) Energetics of repacking a protein interior. Proc. natn. Acad. Sci. U.S.A. 88, 1706-1710.
31. Sandberg W. S. and Terwilliger T. C. (1993) Engineering multiple properties of a protein by combinatorial mutagenesis. Proc. natn. Acad. Sci. U.S.A. 90, 8367-8371.
32. Sawyer J. R. and Blattner F. R. (1991) Rapid detection of antigen binding by antibody fragments expressed in the periplasm of Escherichia coli. Prot. Eng. 4, 947-953.
33. Schildbach J. F., Near R. I., Bruccoleri R. E., Haber E., Jeffrey P. D., Novotny J., Sheriff S. and Margolies M. N. (1993) Modulation of antibody affinity by a non-contact residue. Prot. Sci. 2, 206-214.
34. Schreiber G. and Fersht A. R. (1995) Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J. Mol. Biol. 248, 478-486.
35. Serrano L., Day A. G. and Fersht A. R. (1993) Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. J. Mol. Biol. 233, 305-312.
36. Sharon J. (1990) Structural correlates of high antibody affinity: three engineered amino acid substitutions can increase the affinity of an anti-p-azophenylarsonate antibody 200-fold. Proc. natn. Acad. Sci. U.S.A. 87, 4814-4817.
37. Soberon X., Covarrubias L. and Bolivar F. (1980) Construction and characterization of new cloning vehicles. IV. Deletion derivatives of pBR322 and pBR325. Gene 9, 287-305.
38. Sturtevant J. M. (1994) The thermodynamic effects of protein mutations. Curr. Opin. Struct. Biol. 4, 69-78.
39. Thompson J., Pope T., Tung J.-S., Chan C., Hollis G., Mark G. and Johnson K. S. (1996) Affinity maturation of a high-affinity human monoclonal antibody against the third hypervariable loop of human immunodeficiency virus: use of phage display to improve affinity and broaden strain reactivity. J. Mol. Biol. 256, 77-88.
40. Wells J. A. (1990) Additivity of mutational effects in proteins. Biochemistry 29, 8509-8517.
41. Wong Y. W., Kussie P. H., Parhami-Seren B. and Margolies M. N. (1995) Modulation of antibody affinity by an engineered amino acid substitution, J. Immun. 154, 3351-3358.
42. Xiang J., Chen Z., Delbaere L. T. and Liu E. (1993) Differences in antigen-binding affinity caused by a single amino acid substitution in the variable region of the heavy chain. Immun. Cell Biol. 71 (Part 4), 239-247.
43. Xiang J., Sha Y., Jia Z., Prasad L. and Delbaere L. T. J. (1995) Framework residues 71 and 93 of the chimeric B72.3 antibody are major determinants of the conformation of heavy-chain hypervariable loops. J. Mol. Biol. 253, 385-390.
44. Yang W. P., Green K., Pinz-Sweeney S., Briones A. T., Burton D. R. and Barbas III C. F. (1995) CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J. Mol. Biol. 254, 392-403.
45. Zoller M. J. and Smith M. (1982) Oligonucleotide-directed mutagenesis using M13-derived vectors: an efficient and general procedure for the production of point mutations in any fragment of DNA. Nucl. Acids Res. 10, 6487-6500.