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International Immunology, Vol. 15, No. 3, pp. 417-426, March 2003
© 2003 Japanese Society for Immunology

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

Masayuki Oda1, Haruo Kozono1, Hisayuki Morii2 and Takachika Azuma1

1 Research Institute for Biological Sciences, Tokyo University of Science, 2669 Noda, Chiba 278-0022, Japan 2 National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8566, Japan

Correspondence to: T. Azuma; E-mail: tazuma{at}rs.noda.tus.ac.jp
Transmitting editor: K. Okumura

We have addressed the question of whether antigen binding induces a conformational change in the heavy chain constant (CH) domain of antibodies using staphylococcal protein A or streptococcal protein G as probes, since these proteins are known to bind to IgG domains such as CH1 and CH2–CH3 domains. Biosensor assays on interactions between these proteins and mouse IgG specific to (4-hydroxy-3-nitrophenyl)acetyl (NP) or their enzymatic fragments conducted in the presence or absence of the hapten, NP-{epsilon}-aminocaproic acid (NP-Cap), showed that the binding of IgG to these proteins was inhibited by the binding of NP-Cap. The results of isothermal titration calorimetry also revealed that the association constant for the interaction of protein A with IgG2b decreased by the addition of NP-Cap. These results suggested that antigen binding induced conformational changes in binding sites for protein G or protein A located at CH1 and CH2–CH3 domains, respectively.

Keywords: binding affinity, isothermal titration calorimetry, staphylococcal protein A, streptococcal protein G, surface plasmon resonance biosensor


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