Kinetic analysis of the effect on Fab binding of identical substitutions in a peptide and its parent protein

Biochemistry

Volumn 38, Issue 12, 1999, Pages 3530-3537

  Choulier, Laurence ^a   Rauffer Bruyère, Nathalie ^a,c   Khalifa, Myriam Ben ^b   Martin, Franck ^a   Vernet, Thierry ^b   Altschuh, Danièle ^a  

^a INST DE BIOL MOLEC ET CELLULAIRE   (France)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c NORTHERN ILLINOIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; IMMUNOGLOBULIN F(AB) FRAGMENT;

AMINO ACID SUBSTITUTION; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; CROSS REACTION; DRUG SYNTHESIS; KINETICS; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS; VACCINE PRODUCTION;

ANTIBODY AFFINITY; ANTIBODY SPECIFICITY; BINDING SITES; CAPSID PROTEINS; CIRCULAR DICHROISM; CROSS REACTIONS; EPITOPES, B-LYMPHOCYTE; IMMUNOGLOBULIN FAB FRAGMENTS; KINETICS; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PROTEIN CONFORMATION; VIRAL PROTEINS;

NICOTIANA TABACUM; TOBACCO MOSAIC VIRUS;

EID: 0033596904     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982011z     Document Type: Article

References (65)

1. Lerner, R. A. (1984) Adv. Immunol. 36, 1-44.
2. Roberts, V. A., Getzoff, E. D., and Tainer, J. A. (1993) in Structure of antigens II (Van Regenmortel, M. H. V., Ed.) pp 31-53, Telford and CRC Press, Boca Raton, FL.
3. Van Regenmortel, M. H. V. (1999) J. Immunol. Methods (in press).
4. Geysen, H. M., Rodda, S. J., Mason, T. J., Tribbick, G., and Schoofs, P. G. (1987) J. Immunol. Methods 102, 259-274.
5. Getzoff, E. D., Geysen, H. M., Rodda, S. J., Alexander, H., Tainer, J. A., and Lerner, R. A. (1987) Science 235, 1191-1196.
6. Altschuh, D., Dubs, M. C., Weiss, E., Zeder-Lutz, G., and Van Regenmortel, M. H. V. (1992) Biochemistry 31, 6298-6304.
7. Volkmer-Engert, R., Ehrhard, B., Hellwig, J., Kramer, A., Höhne, W., and Schneider-Mergener, J. ( 1994) Lett. Pept. Sci. 1, 243-253.
8. Rondard, P., Goldberg, M. E., and Bedouelle, H. (1997) Biochemistry 36, 8962-8968.
9. Getzoff, E. D., Tainer, J. A., Lerner, R. A., and Geysen, H. M. (1988) Adv. Immunol. 43, 1-98.
10. Arnon, R., and Van Regenmortel, M. H. V. (1992) FASEB J. 6, 3265-3274.
11. Nicholson, B. H. (1994) Synthetic vaccines, Blackwell Scientific Publications, Oxford, England.
12. Stanfield, L. R., Fieser, T. M., Lerner, R. A., and Wilson, I. A. (1990) Science 248, 712-719.
13. Wien, M. W., Filman, D. J., Stura, E. A., Guillot, S., Delpeyroux, F., Crainic, R., and Hogle, J. M. (1995) Nat. Struct. Biol. 2, 232-243.
14. Lescar, J., Stouracova, R., Riottot, M.-M., Chitarra, V., Brynda, J., Fabry, M., Horejsi, M., Sedlacek, J., and Bentley, G. A. (1997) J. Mol. Biol. 267, 1207-1222.
15. Molins, M. A., Contreras, M. A., Fita, I., and Pons, M. (1998) J. Pept. Sci. 4, 101-110.
16. Rini, J. M., Schulze-Gahmen, U., and Wilson, I. A. (1992) Science 255, 959-965.
17. Tsang, P., Rance, M., Fieser, T. M., Ostresh, J. M., Houghten, R. A., Lerner, R. A., and Wright, P. E. (1992) Biochemistry 31, 3862-3871.
18. Shoham, M. (1993) J. Mol. Biol. 232, 1169-1175.
19. Tormo, J., Blaas, D., Parry, N. R., Rowlands, D., Stuart, D., and Fita, I. (1994) EMBO J. 13, 2247-2256.
20. Davies, D. R., Sheriff, S., and Padlan, E. (1989) Cold Spring Harbor Symp. Quant. Biol. 54, 233-238.
21. Tulip, W. R., Varghese, J. N., Laver, W. G., Webster, R. G., and Colman, P. M. (1992) J. Mol. Biol. 227, 122-148.
22. Malby, R. L., Tulip, W. R., Harley, V. R., McKimm-Breschkin, J. L., Laver, W. G., Webster, R. G., and Colman, P. M. (1994) Structure 15, 733-746.
23. Bossart-Whitaker, P., Chang, C. Y., Novotny, J., Benjamin, D. C., and Sheriff, S. (1995) J. Mol. Biol. 253, 559-575.
24. Cohen, G. H., Sheriff, S., and Davies, D. R. (1996) Acta Crystallogr. D52, 315-326.
25. Scherf, T., Hiller, R., Naider, F., Levitt, M., and Anglister, J. (1992) Biochemistry 31, 6884-6897.
26. Dyson, H. J., and Wright, P. E. (1995) FASEB J. 9, 37-42.
27. Dyson, H. J., Cross, K. J., Houghten, R. A., Wilson, I. A., Wright, P. E., and Lerner, R. A. (1985) Nature 318, 480-483.
28. Dyson, H. J., Rance, M., Houghten, R. A., Lerner, R. A., and Wright, P. E. (1988) J. Mol. Biol. 201, 161-200.
29. Chandrasekhar, K., Profy, A. T., and Dyson, H. J. (1991) Biochemistry 30, 9187-9194.
30. Schulze-Gahmen, U., Rini, J. M., and Wilson, I. A. (1993) J. Mol. Biol. 234, 1098-1118.
31. Zvi, A., Feigelson, D. J., Hayek, Y., and Anglister, J. (1997) Biochemistry 36, 8619-8627.
32. Cheetham, J. C., Raleigh, D. P., Griest, R. E., Redfield, C., Dobson, C. M., and Rees, A. R. (1991) Proc. Natl. Acad. Sci U.S.A. 88, 7968-7972.
33. Mani, J. C., Marchi, V., and Cucurou, C. (1994) Mol. Immunol 31, 439-444.
34. Rondard, P., Brégégère, F., Lecroisey, A., Delepierre, M., and Bedouelle, H. (1997) Biochemistry 36, 8954-8961.
35. Foote, J., and Milstein, C. (1991) Nature 352, 530-532.
36. Foote, J., and Eisen, H. N. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 1254-1256.
37. Al Moudallal, Z., Briand, J. P., and Van Regenmortel, M. H. V. (1985) EMBO J. 4, 1231-1235.
38. Bloomer, A. C., Champness, J. A., Bricogne, G., Staden, R., and Klug, A. (1978) Nature 276, 362-368.
39. Mondragon, A. (1984) Ph.D. Thesis. University of Cambridge, U.K.
40. Chatellier, J., Rauffer-Bruyère, N., Van Regenmortel, M. H. V., Weiss, E., and Altschuh, D. (1996) J. Mol. Recognit. 9, 39-51.
41. Al Moudallal, Z., Briand, J. P., and Van Reeenmortel, M. H. V. (1982) EMBO J. 1, 1005-1010.
42. Richalet-Sécordel, P. M., Rauffer-Bruyère, N., Christensen, L. L. H., Ofenloch-Haehnle, B., Seidel, C., and Van Regenmortel, M. H. V. (1997) Anal. Biochem. 249, 165-173.
43. Chatellier, J., Van Regenmortel, M. H. V., Vernet, T., and Altschuh, D. (1996) J. Mol. Biol. 264, 1-6.
44. Hwang, D.-J., Roberts, I. M., and Wilson, T. M. A. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 9067-9071.
45. Hochuli, E., BannWarth, W., Döbeli, H., Gentz, R., and Stüber, D. (1988) Bio/Technology 6, 1321-1325.
46. Zaitlin, M., and Ferns, W. R. (1964) Science 143, 1451-1452.
47. Kunkel, T. A. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 488-492.
48. Vieira, J., and Messing, J. (1987) Methods Enzymol. 153, 3-11.
49. Studier, F. W., Rosenberg, A. H., Dunn, J. J., and Dubendorff, J. W. (1990) Methods Enzymol. 185, 60-89.
50. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular cloning: A laboratory manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
51. Towbin, H., Staehelin, T., and Gordon, J. (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354.
52. Lofas, S., and Johnsson, B. (1990) J. Chem. Soc., Chem. Commun. 21, 1526-1528.
53. Christensen, L. H. (1997) Anal. Biochem. 249, 153-164.
54. Karlsson, R., Roos, H., Fägerstam, L., and Persson, B. (1994) Methods: Comput. Methods Enzymol. 6, 99-110.
55. O'Shannessy, D. J., Brigham-Burke, M., Soneson, K. K., Hensley, P., and Brooks, I. (1993) Anal. Biochem. 212, 457-468.
56. Roden, L. D., and Myszka, D. G. (1996) Biochem. Biophys. Res. Commun. 225, 1073-1077.
57. Karlsson, R., and Fält, A. (1997) J. Immunol. Methods 200, 121-133.
58. Saunai, H. (1995) Ph.D. Thesis, University Louis Pasteur, Strasbourg, France.
59. Saunal, H., Witz, J., and Van Regenmortel, M. H. V. (1993) J. Gen. Virol. 74, 897-900.
60. Lehrman, S. R., Tuls, J. L., and Lund, M. (1990) Biochemistry 29, 5590-5596.
61. Alexander, H., Alexander, S., Getzoff, E. D., Tainer, J. A., Geysen, H. M., and Lerner, R. A. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 3352-3356.
62. Rondard, P., and Bedouelle, H. (1999) J. Biol. Chem. (in press).
63. Burgen, A. S. V., Roberts, G. C. K., and Feeney, J. (1975) Nature 253, 753-755.
64. Malmqvist, M. (1994) J. Mol. Recognit. 7, 1-7.
65. Doyle, M. L., Myszka, D. G., and Chaiken, I. M. (1996) J. Mol. Recognit. 9, 65-74.