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Biochemical Features of a Catalytic Antibody Light Chain, 22F6, Prepared from Human Lymphocytes


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タイトル: Biochemical Features of a Catalytic Antibody Light Chain, 22F6, Prepared from Human Lymphocytes
著者: Hifumi, Emi / Fujimoto, Naoko / Arakawa, Mitsue / Saito, Eri / Matsumoto, Shingo / Kobayashi, Nobuyuki / Uda, Taizo
発行日: 2013年 7月 5日
出版者: American Society for Biochemistry and Molecular Biology Inc.
引用: Journal of Biological Chemistry, 288(27), pp.19558-19568; 2013
抄録: Human antibody light chains belonging to subgroup II of germ line genes were amplified by a seminested PCR technique using B-lymphocytes taken from a human adult infected with influenza virus. Each gene of the human light chains was transferred into the Escherichia coli system. The recovered light chain was highly purified using a two-step purification system. Light chain 22F6 showed interesting catalytic features. The light chain cleaved a peptide bond of synthetic peptidyl-4-methylcoumaryl- 7-amide (MCA) substrates, such as QAR-MCA and EAR-MCA, indicating amidase activity. It also hydrolyzed a phosphodiester bond of both DNA and RNA. From the analysis of amino acid sequences and molecular modeling, the 22F6 light chain possesses two kinds of active sites as amidase and nuclease in close distances. The 22F6 catalytic light chain could suppress the infection of influenza virus type A (H1N1) of Madin-Darby canine kidney cells in an in vitro assay. In addition, the catalytic light chain clearly inhibited the infection of the influenza virus of BALB/c mice via nasal administration in an in vivo assay. In the experiment, the titer in the serum of the mice coinfected with the 22F6 light chain and H1N1 virus became considerably lowered compared with that of 22F6-non-coinfected mice. Note that the catalytic light chain was prepared from human peripheral lymphocyte and plays an important role in preventing infection by influenza virus. Considering the fact that the human light chain did not show any acute toxicity for mice, our procedure developed in this study must be unique and noteworthy for developing new drugs.
URI: http://hdl.handle.net/10069/33594
ISSN: 00219258
DOI: 10.1074/jbc.M113.454579
権利: © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. / This is author's choice open-access article distributed under the terms of the Creative Commons Attribution License.
資料タイプ: Journal Article
原稿種類: publisher
出現コレクション:050 学術雑誌論文

引用URI : http://hdl.handle.net/10069/33594

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