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The Fab portion of immunoglobulin G contributes to its binding to Fcγ receptor III.
Yogo, Rina; Yamaguchi, Yuki; Watanabe, Hiroki; Yagi, Hirokazu; Satoh, Tadashi; Nakanishi, Mahito; Onitsuka, Masayoshi; Omasa, Takeshi; Shimada, Mari; Maruno, Takahiro; Torisu, Tetsuo; Watanabe, Shio; Higo, Daisuke; Uchihashi, Takayuki; Yanaka, Saeko; Uchiyama, Susumu; Kato, Koichi.
Affiliation
  • Yogo R; Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, 444-8787, Japan.
  • Yamaguchi Y; Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, Aichi, 467-8603, Japan.
  • Watanabe H; Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  • Yagi H; Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, 444-8787, Japan.
  • Satoh T; Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, Aichi, 467-8603, Japan.
  • Nakanishi M; Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, Aichi, 467-8603, Japan.
  • Onitsuka M; Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Central 5, Tsukuba, Ibaraki, 305-8565, Japan.
  • Omasa T; Graduate School of Technology, Industrial and Social Sciences, Tokushima University, Minamijosanjima-cho 2-1, Tokushima, 770-8513, Japan.
  • Shimada M; Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  • Maruno T; Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  • Torisu T; Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  • Watanabe S; Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  • Higo D; Thermo Fisher Scientific, 3-9 Moriya-cho, Kanagawa-ku, Yokohama-shi, Kanagawa, 221-0022, Japan.
  • Uchihashi T; Thermo Fisher Scientific, 3-9 Moriya-cho, Kanagawa-ku, Yokohama-shi, Kanagawa, 221-0022, Japan.
  • Yanaka S; Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, 444-8787, Japan.
  • Uchiyama S; Department of Physics, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi, 464-8602, Japan.
  • Kato K; Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, 444-8787, Japan.
Sci Rep ; 9(1): 11957, 2019 08 16.
Article in En | MEDLINE | ID: mdl-31420591
Most cells active in the immune system express receptors for antibodies which mediate a variety of defensive mechanisms. These receptors interact with the Fc portion of the antibody and are therefore collectively called Fc receptors. Here, using high-speed atomic force microscopy, we observe interactions of human, humanized, and mouse/human-chimeric immunoglobulin G1 (IgG1) antibodies and their cognate Fc receptor, FcγRIIIa. Our results demonstrate that not only Fc but also Fab positively contributes to the interaction with the receptor. Furthermore, hydrogen/deuterium exchange mass spectrometric analysis reveals that the Fab portion of IgG1 is directly involved in its interaction with FcγRIIIa, in addition to the canonical Fc-mediated interaction. By targeting the previously unidentified receptor-interaction sites in IgG-Fab, our findings could inspire therapeutic antibody engineering.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Immunoglobulin G / Immunoglobulin Fab Fragments / Immunoglobulin Fc Fragments / Receptors, IgG / Rituximab Limits: Animals / Humans Language: En Journal: Sci Rep Year: 2019 Document type: Article Affiliation country: Japan Country of publication: United kingdom
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Immunoglobulin G / Immunoglobulin Fab Fragments / Immunoglobulin Fc Fragments / Receptors, IgG / Rituximab Limits: Animals / Humans Language: En Journal: Sci Rep Year: 2019 Document type: Article Affiliation country: Japan Country of publication: United kingdom