Reduction in the amide hydrogen exchange rates of an anti-lysozyme Fv fragment due to formation of the Fv-lysozyme complex

Journal of Molecular Biology

Volumn 270, Issue 5, 1997, Pages 751-762

  Williams Jr , David C ^a   Rule, Gordon S ^b   Poljak, Roberto J ^c   Benjamin, David C ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b CARNEGIE MELLON UNIVERSITY   (United States)

^c UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

Author keywords

Amide hydrogen exchange; Antigen antibody complexes; Nuclear magnetic resonance; Protein dynamics; Structural fluctuations

Indexed keywords

AMIDE; HYDROGEN; LYSOZYME; MONOCLONAL ANTIBODY; NITROGEN 15;

ANTIGEN ANTIBODY COMPLEX; ANTIGEN BINDING; ARTICLE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL;

EID: 0031215027     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1122     Document Type: Article

References (41)

1. Amit A. G., Mariuzza R. A., Phillips S. E. V., Poljak R. J. Three dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science. 233:1986;747-753.
2. Anglister J., Frey T., McConnell H. M. NMR techniques for assessing contributions of heavy and light chains to an antibody combining site. Nature. 315:1985;65-67.
3. Banerjee S. K., Pogolotti A. Jr, Rupley J. A. Self-association of lysozyme. J. Biol. Chem. 250:1975;8260-8266.
4. Benjamin D. C., Williams D. C. Jr, Smith-Gill S. J., Rule G. S. Long-range changes in a protein antigen due to antigen-antibody interaction. Biochemistry. 31:1992;9539-9545.
5. Bhat T. N., Bentley G. A., Fischmann T. O., Boulot G., Poljak R. J. Small rearrangements in structures of Fv and Fab fragments of antibody D1.3 on antigen binding. Nature. 347:1990;483-485.
6. Bhat T. N., Bentley G. A., Boulot G., Greene M. I., Tello D., Dall'Acqua W., Souchon H., Schwarz F. P., Mariuzza R. A., Poljak R. J. Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Proc. Natl Acad. Sci. USA. 91:1994;1089-1093.
7. Boulot G., Eisele J., Bentley G. A., Bhat T. N., Ward E. S., Winter G., Poljak R. J. Crystallization and preliminary X-ray diffraction study of the bacterially expressed Fv from the monoclonal anti-lysozyme antibody D1.3 and of its complex with the antigen, lysozyme. J. Mol. Biol. 213:1990;617-619.
8. Braden B. C., Poljak R. J. Structural features of the reaction between antibodies and protein antigens. FASEB J. 9:1995;9-16.
9. Braden B. C., Fields B. A., Ysern X., Goldbaum F. A., Dall'Acqua W., Schwarz F. P., Poljak R. J., Mariuzza R. A. Crystal structure of the complex of the variable-domain of antibody D1.3 and turkey egg white lysozyme: a novel conformational change in antibody CDR-L3 selects for antigen. J. Mol. Biol. 257:1996;889-894.
10. Briercheck D. M., Allison T. J., Richardson J. P., Ellena J. F., Wood T. C., Rule G. S. H-1, N-15, and C-13 resonance assignments and secondary structure determination of the RNA-binding domain of E. coli rho protein. J. Biomol. NMR. 8:1996;429-444.
11. αcross peaks in 15N- and 13C-labeled proteins. J. Biomol. NMR. 2:1992;203-210.
12. Davies D. R., Padlan E. A., Sheriff S. Antibody-antigen complexes. Annu. Rev. Biochem. 59:1990;439-473.
13. Englander S. W., Englander J. J., McKinnie R. E., Ackers G. K., Turner G. J., Westrick J. A., Gill S. J. Hydrogen exchange measurements of the free energy of structural and allosteric change in hemoglobin. Science. 256:1992;1684-1687.
14. Fields B. A., Goldbaum F. A., Ysern X., Poljak R. J., Mariuzza R. A. Molecular basis of antigen mimicry by an anti-idiotope. Nature. 374:1995;739-742.
15. Goldbaum F. A., Schwarz F. P., Eisenstein E., Cauerhff A., Mariuzza R. A., Poljak R. J. The effect of water activity on the association constant and the enthalpy of reaction between lysozyme and the specific antibodies D1.3 and D44.1. J. Mol. Recogn. 9:1996;6-12.
16. Grzesiek S., Bax A. Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J. Magn. Reson. 96:1992a;432-440.
17. Grzesiek S., Bax A. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114:1992b;6291-6293.
18. Grzesiek S., Bax A. Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. J. Biomol. NMR. 3:1993;185-204.
19. Hayashi K., Imote T., Funatsu G., Funatsu M. The position of the active tryptophan residue in lysozyme. J. Biochem. (Tokyo). 58:1965;227-235.
20. Johnson M. L., Frasier S. G. Nonlinear least-squares analysis. Methods Enzymol. 117:1985;301-342.
21. Kay L. E., Ikura M., Tschudin R., Bax A. Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89:1990;496-514.
22. Kelley R. F., O'Connell M. P. Thermodynamic analysis of an antibody functional epitope. Biochemistry. 32:1993;6828-6835.
23. Loh S. N., Prehoda K. E., Wang J., Markley J. L. Hydrogen exchange in unliganded and liganded Staphylococcal nuclease. Biochemistry, 32:1993;11022-11028.
24. 15N-labeled proteins. J. Am. Chem. Soc. 111:1989;1515-1517.
25. Mayne L., Paterson Y., Cerasoli D., Englander S. W. Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR. Biochemistry. 31:1992;10678-10685.
26. Miller D. W., Dill K. A. A statistical mechanical model for hydrogen exchange in globular proteins. Protein Sci. 4:1995;1860-1873.
27. Murphy K. P., Friere E., Patterson Y. Configurational effects in antibody-antibody-antigen interactions studied by microcalorimetry. Proteins: Struct. Funct. Genet. 21:1995;83-90.
28. Novotny J., Sharp K. Electrostatic fields in antibodies and antibody/antigen complexes. Prog. Biophys. Mol. Biol. 58:1992;203-224.
29. Novotny J., Bruccoleri R. E., Saul F. A. On the attribution of binding energy in antigen-antibody complexes McPC 603, D1.3, and HyHEL-5. Biochemistry. 28:1989;4735-4749.
30. Orban J., Alexander P., Bryan P. Hydrogen-deuterium exchange in the free and immunoglobulin G bound protein GB-domain. Biochemistry. 33:1994;5702-5710.
31. Paterson Y., Englander S. W., Roder H. An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR. Science. 249:1990;755-759.
32. Privalov P. L., Tsalkova T. N. Micro- and macro-stabilities of globular proteins. Nature, 280:1979;693-696.
33. Rizzo P., Tinello C., Punturieri A., Taniuchi H. A study of hydrogen exchange of monoclonal antibodies: specificity of the antigen-binding induced conformational stabilization. Biochim. Biophys. Acta. 1159:1992;1669-1678.
34. Schwarz F. P., Tello D., Goldbaum F. A., Mariuzza R. A., Poljak R. J. Thermodynamics of antigen-antibody binding using specific anti-lysozyme antibodies. Eur. J. Biochem. 228:1995;388-394.
35. Shindo H., Cohen J. S., Rupley J. A. Self-association of hen egg-white lysozyme as studied by nuclear magnetic resonance. Biochemistry. 16:1977;3879-3882.
36. States D. J., Haberkorn R. A., Ruben D. J. A 2-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Reson. 48:1982;286-292.
37. Takahashi H., Odaka A., Kawaminami S., Matsunaga C., Kato K., Shimada I., Arata Y. Multinuclear NMR study of the structure of the Fv fragment of anti-dansyl mouse IgG2a antibody. Biochemistry. 30:1991;6611-6619.
38. 15N shift correlation NMR spectroscopy. Biochemistry. 31:1992;2464-2468.
39. Williams D. C. Jr, Benjamin D. C., Poljak R. J., Rule G. S. Global changes in amide hydrogen exchange rates for a protein antigen in complex with three different antibodies. J. Mol. Biol. 257:1996;866-876.
40. Woodward C. K., Simon L., Tuchsen E. Hydrogen exchange and the dynamic structure of proteins. Mol. Cell. Biochem. 48:1982;135-160.
41. Wright P. E., Dyson H. J., Lerner R. A., Riechmann L., Tsang P. Antigen-antibody interactions: an NMR approach. Biochem. Pharmacol. 40:1990;83-88.