Crystal structure of streptavidin mutant with low immunogenicity.

Authors:
Tatsuya Kawato
Tatsuya Kawato
Boston | United States
Eiichi Mizohata
Eiichi Mizohata
Osaka University
Japan
Tomohiro Meshizuka
Tomohiro Meshizuka
Graduate School of Engineering
Boston | United States
Hirofumi Doi
Hirofumi Doi
The University of Tokyo
Bunkyo | Japan
Takeshi Kawamura
Takeshi Kawamura
Research Center for Advanced Science and Technology
Japan
Hiroyoshi Matsumura
Hiroyoshi Matsumura
Osaka University
Japan
Kyohei Yumura
Kyohei Yumura
The University of Tokyo
Japan
Kouhei Tsumoto
Kouhei Tsumoto
School of Engineering

J Biosci Bioeng 2015 Jun 26;119(6):642-7. Epub 2014 Nov 26.

Radioisotope Center, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. Electronic address:

We previously created a low-immunogenic core streptavidin mutant No. 314 (LISA-314) by replacing six amino-acid residues for use as a delivery tool for an antibody multistep pre-targeting process (Yumura et al., Protein Sci., 22, 213-221, 2013). Here, we performed high-resolution X-ray structural analyses of LISA-314 and wild-type streptavidin to investigate the effect of substitutions on the protein function and the three-dimensional structure. LISA-314 forms a tetramer in the same manner as wild-type streptavidin. The binding mode of d-biotin in LISA-314 is also completely identical to that in wild-type streptavidin, and conformational changes were observed mostly at the side chains of substituted sites. Any large conformational changes corresponding to the reduction of B factors around the substituted sites were not observed. These results demonstrated the LISA-314 acquired low immunogenicity without losing structural properties of original wild-type streptavidin.
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June 2015
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