Evidence of allosteric conformational changes in the antibody constant region upon antigen binding

International Immunology

Volumn 15, Issue 3, 2003, Pages 417-426

  Oda, Masayuki ^a   Kozono, Haruo ^a   Morii, Hisayuki ^b   Azuma, Takachika ^a  

^a TOKYO UNIVERSITY OF SCIENCE   (Japan)

^b Advanced Industrial Science Technol   (Japan)

Author keywords

Binding affinity; Isothermal titration calorimetry; Staphylococcal protein A; Streptococcal protein G; Surface plasmon resonance biosensor

Indexed keywords

ACETIC ACID DERIVATIVE; AMINOCAPROIC ACID; HAPTEN; IMMUNOGLOBULIN G2B; IMMUNOGLOBULIN HEAVY CHAIN; PROTEIN G; RECOMBINANT PROTEIN; STAPHYLOCOCCUS PROTEIN A;

ALLOSTERISM; ANTIBODY COMBINING SITE; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; BIOSENSOR; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; IMMUNOGLOBULIN CONSTANT REGION; PRIORITY JOURNAL; PROTEIN INTERACTION; TITRIMETRY;

ALLOSTERIC REGULATION; ANIMALS; ANTIGENS, BACTERIAL; BINDING SITES, ANTIBODY; IMMUNOGLOBULIN G; MICE; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 0037342172     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/dxg036     Document Type: Article

References (37)

1. Davies, D. R. and Metzger, H. 1983. Antibody-antigen complexes. Annu. Rev. Immunol. 1:87.
2. Jefferis, R., Lund, J. and Pound, J. D. 1998. IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation. Immunol. Rev. 163:59.
3. Wilson, I. A. and Stanfield, R. L. 1994. Antibody-antigen interactions: new structures and new conformational changes. Curr. Opin. Struct. Biol. 4:857.
4. Langone, J. J. 1982. Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumonococci. Adv. Immunol. 32:157.
5. Silverman, G. J. 1997. B-cell superantigens. Immunol. Today 18:379.
6. Uhlén, M., Guss, B. Nilsson, B. Gatenbeck, S. Philipson, L. and Lindberg, M. 1984. Complete sequence of the staphylococcal gene encoding protein A. A gene evolved through multiple duplications. J. Biol. Chem. 259:1695.
7. Jansson, B., Uhlén, M. and Nygren, P. A. 1998. All individual domains of staphylococcal protein A show Fab binding. FEMS Immunol. FEMS Immunol. Med. Microbiol. 20:69.
8. Deisenhofer, J. 1981. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution. Biochemistry 20:2361.
9. Graille, M., Stura, E. A., Corper, A. L., Sutton, B. J., Taussig, M. J., Charbonnier, J. B. and Silverman, G. J. 2000. Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity. Proc. Natl Acad. Sci. USA 97:5399.
10. Lian, L.-Y., Barsukov, I. L., Derrick, J. P. and Roberts, G. C. 1994. Mapping the interactions between streptococcal protein G and the Fab fragment of IgG in solution. Nat. Struct. Biol. 1:355.
11. Gronenborn, A. M. and Clore, G. M. 1993. Identification of the contact surface of a streptococcal protein G domain complexed with a human Fc fragment. J. Mol. Biol. 233:331.
12. Sauer-Eriksson, A. E., Kleywegt, G. J., Uhlén, M. and Jones, T. A. 1995. Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure 3:265.
13. Derrick, J. P. and Wigley, D. B. 1992. Crystal structure of a streptococcal protein G domain bound to an Fab fragment. Nature 359:752.
14. Derrick, J. P. and Wigley, D. B. 1994. The third IgG-binding domain from streptococcal protein G. An analysis by X-ray crystallography of the structure alone and in a complex with Fab. J. Mol. Biol. 243:906.
15. Oda, M. and Nakamura, H. 2000. Thermodynamic and kinetic analyses for understanding sequence-specific DNA recognition, Genes to Cells 5:319.
16. Oda, M. and Azuma, T. 2000. Reevaluation of stoichiometry and affinity/avidity in interactions between anti-hapten antibodies and mono- or multi-valent antigens. Mol. Immunol. 37:1111.
17. Taketani, M., Naitoh, A., Motoyama, N. and Azuma, T. 1995. Role of conserved amino acid residues in the complementarity determining regions on hapten-antibody interaction of anti-(4-hydroxy-3-nitrophenyl) acetyl antibodies. Mol. Immunol. 32:983.
18. Furukawa, K., Akasako-Furukawa, A., Shirai, H., Nakamura, H. and Azuma, T. 1999. Junctional amino acids determine the maturation pathway of an antibody. Immunity 11:329.
19. Terauchi, A., Hayashi, K., Kitamura, D., Kozono, Y., Motoyama, N. and Azuma, T. 2001. A pivotal role for DNase I-sensitive regions 3b and/or 4 in the induction of somatic hypermutation of IgH genes. J. Immunol. 167:811.
20. Olsson, A., Eliasson, M., Guss, B., Nilsson, B., Hellman, U., Lindberg, M. and Uhlén, M. 1987. Structure and evolution of the repetitive gene encoding streptococcal protein G. Eur. J. Biochem. 168:319.
21. Morii, H., Uedaira, H., Ogata, K., Ishii, S. and Sarai, A. 1999. Shape and energetics of a cavity in c-Myb probed by natural and non-natural amino acid mutations. J. Mol. Biol. 292:909.
22. Karlsson, R., Mo, J. A. and Holmdahl, R. 1995. Binding of autoreactive mouse anti-type II collagen antibodies derived from the primary and the secondary immune response investigated with the biosensor technique. J. Immunol. Methods 188:63.
23. HIII H chains. J. Immunol. 142:2778.
24. γ3 interface region of IgG and is related to the sites that bind staphylococcal protein A and human rheumatoid factors. J. Immunol. 143:565.
25. Chou, C.-L. and Sadegh-Nasseri, S. 2000. HLA-DM recognizes the flexible conformation of major histocompatibility complex class II. J. Exp. Med. 192:1697.
26. H III related 7183, J606 and S107 and DNA4 families commonly encode for binding to a bacterial B cell superantigen. Mol. Immunol. 36:769.
27. Tashiro, M. and Montelione, G. T. 1995. Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins. Curr. Opin. Struct. Biol. 5:471.
28. Edelman, G. M. 1970. The covalent structure of a human γG-immunoglobulin. XI. Functional implications. Biochemistry 16:3197.
29. Mizutani, R., Miura, K., Nakayama, T., Shimada, I., Arata, Y. and Satow, Y. 1995. Three-dimensional structures of the Fab fragment of murine N1G9 antibody from the primary immune response and of its complex with (4-hydroxy-3-nitrophenyl)acetate. J. Mol. Biol. 254:208.
30. Guddat, L. W., Shan, L., Anchin, J. M., Linthicum, D. S. and Edmundson, A. B. 1994. Local and transmitted conformational changes on complexation of an anti-sweetener Fab. J. Mol. Biol. 236:247.
31. Davies, D. R., Padlan, E. A. and Sheriff, S. 1990. Antibody-antigen complexes. Annu. Rev. Biochem. 59:439.
32. Harris, L. J., Larson, S. B. and McPherson, A. 1999. Comparison of intact antibody structures and the implications for effector function. Adv. Immunol. 72:191.
33. Kravchuk, Z. I., Chumanevich, A. A., Vlasov, A. P. and Martsev, S. P. 1998. Two high-affinity monoclonal IgG2a antibodies with differing thermodynamic stability demonstrate distinct antigen-induced changes in protein A-binding affinity. J. Immunol. Methods 217:131.
34. Starovasnik, M. A., O'Connell, M. P., Fairbrother, W. J. and Kelley, R. F. 1999. Antibody variable region binding by Staphylococcal protein A: thermodynamic analysis and location of the Fv binding site on E-domain. Protein Sci. 8:1423.
35. Schlessingers, J., Steinberg, I. Z., Givol, D., Hochman, J. and Pecht, I. 1975. Antigen-induced conformational changes in antibodies and their Fab fragments studied by circular polarization of fluorescence. Proc. Natl Acad. Sci. USA 72:2775.
36. Hsieh, H. V., Poglitsch, C. L. and Thompson, N. L. 1992. Direct measurement of the weak interactions between a mouse Fc receptor (FcγRII) and IgG1 in the absence and presence of hapten: a total internal reflection fluorescence microscopy study. Biochemistry 31:11562.
37. Burmeister, W. P., Huber, A. H. and Bjorkman, P. J. 1994. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 372:379.