| 研究実績の概要 |
In this year we have made progress in various fronts. The study of the effect of glycosylation in an antibody has been advanced, and we have corroborated the effect of CH2 glycosylation, supporting previous results and strengthening our hypothesis.
Second, we have further our understanding of recognition of antigens by antibodies under various relevant conditions, in particular the role of interfaces and epitopes at interfaces. This idea has been promoted in the clinically important target HIV-1, and also in another disease relsated to the hemolytic syndrome.
Finally, we have advanced greatly the understanding of the hinge region in connection with the dimerization stability of IgG1, and how this influences the binding to Fc receptors. This work is very novel and will be published in the near future. and presented at the Japanese Protein Society meeting. Site-directed mutagenesis in this region has pointed to specific residues that change the local structure leading to a unexpectedly weak IgG that however is able to recognize the Fc receptor. The results have been corroborated by surface plasmon resonance, including two types of Fc receptors. In addition, the effect of the antogen bound to the antibody has also been verified.
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