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Protein Engineering, Vol. 16, No. 4, 243-245, April 2003
© 2003 Oxford University Press

COMMUNICATION

Single amino acid substitution in the mouse IgG1 Fc region induces drastic enhancement of the affinity to protein A

Masato Nagaoka and Toshihiro Akaike1

Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan

1 To whom correspondence should be addressed.E-mail: takaike{at}bio.titech.ac.jp

The purification of monoclonal antibody sometimes requires a lot of time and involves complicated steps because of the poorer ability of mouse IgG to interact with protein A, or also with protein G, than IgGs from other species such as those of human and rabbit. To resolve this problem, we exchanged one or two amino acid residues of mouse IgG Fc region with that of human IgG. Three mutants (T252M, T254S and T252M–T254S) showed significant improvement in the affinity to protein A. The exchange of the threonine 252 residue to methionine (T252M) was most efficient. This result suggests that a direct and simple modification allows the efficient purification of monoclonal antibody and of fusion protein containing mouse IgG Fc region.


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