Binding of peptides in solution by the Escherichia coli chaperone PapD as revealed using an inhibition ELISA and NMR spectroscopy

Bioorganic and Medicinal Chemistry

Volumn 6, Issue 11, 1998, Pages 2085-2101

  Flemmer Karlsson, Katarina ^a   Walse, Björn ^a   Drakenberg, Torbjörn ^a   Roy, Sarbari ^a   Bergquist, Karl Erik ^a   Pinkner, Jerome S ^b   Hultgren, Scott J ^b   Kihlberg, Jan ^c  

^a LUND UNIVERSITY   (Sweden)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UMEÅ UNIVERSITY   (Sweden)

Author keywords

Chaperone; ELISA; NMR spectroscopy; Peptide; Pili; Structure activity

Indexed keywords

CHAPERONE; HYBRID PROTEIN; SYNTHETIC PEPTIDE;

ARTICLE; BACTERIAL VIRULENCE; COMPLEX FORMATION; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE SYNTHESIS; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; ENZYME-LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; INDICATORS AND REAGENTS; KINETICS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; PEPTIDE FRAGMENTS; PERIPLASMIC PROTEINS; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0031768474     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0896(98)00162-X     Document Type: Article

References (63)

1. Hultgren, S. J.; Abraham, S.; Caparon, M.; Falk, P.; St. Geme, J. W., III; Normark, S. Cell 1993, 73, 887.
2. Hung, D. L.; Knight, S. D.; Woods, R. M.; Pinkner, J. S.; Hultgren, S. J. EMBO J. 1996, 15, 3792.
3. Kuehn, M. J.; Heuser, J.; Normark, S.; Hultgren, S. J. Nature 1992, 356, 252.
4. Bullitt, E.; Makowski, L. Nature 1995, 373, 164.
5. Källenius, G.; Möllby, R.; Svenson, S. B.; Winberg, J.; Lundblad, A.; Svensson, S.; Cedergren, B. FEMS Lett. 1980, 7, 297.
6. Leffler, H.; Svanborg Edén, C. FEMS Lett. 1980, 8, 127.
7. Kihlberg, J.; Hultgren, S. J.; Normark, S.; Magnusson, G. J. Am. Chem. Soc. 1989, 111, 6364.
8. Striker, R.; Nilsson, U.; Stonecipher, A.; Magnusson, G.; Hultgren, S. J. Mol. Microbiol. 1995, 16, 1021.
9. Nilsson, U.; Striker, R. T.; Hultgren, S. J.; Magnusson, G. Bioorg. Med. Chem. 1996, 4, 1809.
10. Hultgren, S. J.; Lindberg, F.; Magnusson, G.; Kihlberg, J.; Tennent, J. M.; Normark, S. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 4357.
11. Kuehn, M. J.; Normark, S.; Hultgren, S. J. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 10586.
12. Bullitt, E.; Jones, C. H.; Striker, R.; Soto, G.; Jacob-Dubuisson, F.; Pinkner, J.; Wick, M. J.; Makowski, L.; Hultgren, S. J. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 12890.
13. Holmgren, A.; Brändén, C.-I. Nature 1989, 342, 248.
14. Holmgren, A.; Kuehn, M. J.; Brändén, C.-I.; Hultgren, S. J. EMBO J. 1992, 11, 1617.
15. Kuehn, M. J.; Ogg, D. J.; Kihlberg, J.; Slonim, L. N.; Flemmer, K.; Bergfors, T.; Hultgren, S. J. Science 1993, 262, 1234.
16. Xu, Z.; Jones, C. H.; Haslam, D.; Pinkner, J. S.; Dodson, K.; Kihlberg, J.; Hultgren, S. J. Mol. Microbiol. 1995, 16, 1011.
17. Stephens, C.; Shapiro, L. Chem. Biol. 1997, 4, 637.
18. Flemmer Karlsson, K.; Walse, B.; Drakenberg, T.; Kihlberg, J. Lett. Peptide Sci. 1996, 3, 143.
19. Cameron, L. R.; Holder, J. L.; Meldal, M.; Sheppard, R. C. J. Chem. Soc. Perkin Trans. 1. 1988, 2895.
20. Garegg, P. J.; Samuelsson, B. J. Chem. Soc. Perkin Trans. 1. 1980, 2866.
21. Carpino, L. A.; El-Faham, A.; Minor, C. A.; Albericio, F. J. Chem. Soc., Chem. Commun. 1994, 201.
22. Carpino, L. A. J. Am. Chem. Soc. 1993, 115, 4397.
23. Carpino, L. A.; El-Faham, A. J. Org. Chem. 1994, 59, 695.
24. Flemmer, K.; Xu, Z.; Pinkner, J. S.; Hultgren, S. J.; Kihlberg, J. Bioorg. Med. Chem. Lett. 1995, 5, 927.
25. Derrick, J. P.; Wigley, D. B. Nature 1992, 359, 752.
26. Wüthrich, K. NMR of Proteins and Nucleic Acids; New York: Wiley & Sons, 1986.
27. Dyson, H. J.; Wright, P. E. Annu. Rev. Biophys. Biophys. Chem. 1991, 20, 519.
28. Bundi, A.; Grathwohl, C.; Hochmann, J.; Keller, R. M.; Wagner, G.; Wüthrich, K. J. Magn. Reson. 1975, 18, 191.
29. Wishart, D. S.; Bigham, C. G.; Holm, A.; Hodges, R. S.; Sykes, B. D. J. Biomol. NMR. 1995, 5, 67.
30. Gronenborn, A. M.; Clore, G. M. Crit. Rev. Biochem. Mol. Biol. 1995, 30, 351.
31. Ni, F. Prog. Nucl. Magn. Reson. Spectrosc. 1994, 26, 517.
32. -1 for this octapeptide. Since PapG308-314 is a weaker inhibitor than the octapeptide PapG307-314, the off-rate of PapG308-314 should be even higher, thus corresponding to the fast exchange regime.
33. Neuhaus, D.; Williamson, M. P. The nuclear Overhauser effect in structural and conformational analysis; New York: VCH Publishers, 1989.
34. Walse, B.; Kihlberg, J.; Flemmer Karlsson, K.; Nilsson, M.; Wahlund, K.-G.; Pinkner, J. S.; Hultgren, S. J.; Drakenberg, T. FEBS Lett. 1997, 412, 115.
35. Campbell, A. P.; Sykes, B. D. Annu. Rev. Biophys. Chem. Biomol. Struct. 1993, 22, 99.
36. Kuboniwa, H.; Grzesiek, S.; Delaglio, F.; Bax, A. J. Biomol. NMR. 1994, 4, 871.
37. Smith, L. J.; Bolin, K. A.; Schwalbe, H.; MacArthur, M. W.; Thornton, J. M.; Dobson, C. M. J. Mol. Biol. 1996, 255, 494.
38. The differences in chemical shift observed for some of the residues in PapG308-314 on addition of PapD may appear to be small (0.01 ppm). However, the observed chemical shift is an average of the shift for free and bound peptide. Since a peptide:PapD ratio of 25:1 was used in the NMR studies the ratio between free and bound peptide is >25:1. Thus, the actual chemical shift difference between the free and bound form could be estimated to be ~0.3 ppm, or even greater.
39. Gallop, M. A.; Barrett, R. W.; Dower, W. J.; Fodor, S. P. A.; Gordon, E. M. J. Med. Chem. 1994, 37, 1233.
40. Gordon, E. M.; Barrett, R. W.; Dower, W. J.; Fodor, S. P. A.; Gallop, M. A. J. Med. Chem. 1994, 37, 1385.
41. Thompson, L. A.; Ellman, J. A. Chem. Rev. 1996, 96, 555.
42. Fersht, A. R.; Shi, J. P.; Knill-Jones, J.; Lowe, D. M.; Wilkinson, A. J.; Blow, D. M.; Brick, P.; Carter, P.; Waye, M. M. Y.; Winter, G. Nature 1985, 314, 235.
43. Barlos, K.; Chatzi, O.; Gatos, D.; Stavropoulos, G. Int. J. Peptide Protein Res. 1991, 37, 513.
44. Rink, H. Tetrahedron Lett. 1987, 28, 3787.
45. Bernatowicz, M. S.; Daniels, S. B.; Köster, H. Tetrahedron Lett. 1989, 30, 4645.
46. Aue, W. P.; Bartholdi, E.; Ernst, R. R. J. Chem. Phys. 1976, 64, 2229.
47. Rance, M.; Sorensen, O. W.; Bodenhausen, G.; Wagner, G.; Ernst, R. R.; Wüthrich, K. Biochem. Biophys. Res. Commun. 1983, 117, 479.
48. Braunschweiler, L.; Ernst, R. R. J. Magn. Reson. 1983, 53, 521.
49. Bax, A.; Davis, D. G. J. Magn. Reson. 1985, 65, 355.
50. Davis, D. G.; Bax, A. J. Am. Chem. Soc. 1985, 107, 2820.
51. Jeener, J.; Meier, B. H.; Bachmann, P.; Ernst, R. R. J. Chem. Phys. 1979, 71, 4546.
52. Kumar, A.; Ernst, R. R.; Wüthrich, K. Biochem. Biophys. Res. Comm. 1980, 95, 1.
53. Macura, S.; Ernst, R. R. Mol. Phys. 1980, 41, 95.
54. Bothner-By, A. A.; Stephens, R. L.; Lee, J.-M.; Warren, C. D.; Jeanloz, R. W. J. Am. Chem. Soc. 1984, 106, 811.
55. Bax, A.; Davis, D. G. J. Magn. Reson. 1985, 63, 207.
56. Rance, M. J. Magn. Reson. 1987, 74, 557.
57. Shaka, A. J.; Lee, C. J.; Pines, A. J. Magn. Reson. 1988, 77, 274.
58. States, D. J.; Haberkorn, R. A.; Ruben, D. J. J. Magn. Reson. 1982, 48, 286.
59. Leathers, V. L.; Linse, S.; Forsén, S.; Norman, A. W. J. Biol. Chem. 1990, 265, 9838.
60. Piotto, M.; Saudek, V.; Sklenár, V. J. Biomol. NMR. 1992, 661.
61. Hwang, T.-L.; Shaka, A. J. J. Magn. Reson. A. 1995, 112, 275.
62. Zhang, O.; Kay, L. E.; Olivier, J. P.; Forman-Kay, J. D. J. Biomol. NMR. 1994, 4, 845.
63. Cavanagh, J.; Rance, M. J. Magn. Reson. 1992, 96, 670.