ID | 114953 |
Author |
Yogo, Rina
National Institutes of Natural Sciences|Nagoya City University
Yamaguchi, Yuki
Osaka University
Watanabe, Hiroki
National Institutes of Natural Sciences
Yagi, Hirokazu
Nagoya City University
Satoh, Tadashi
Nagoya City University
Nakanishi, Mahito
National Institute of Advanced Industrial Science and Technology
Onitsuka, Masayoshi
Tokushima University
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Shimada, Mari
Osaka University
Maruno, Takahiro
Osaka University
Torisu, Tetsuo
Osaka University
Watanabe, Shio
Thermo Fisher Scientific
Higo, Daisuke
Thermo Fisher Scientific
Uchihashi, Takayuki
National Institutes of Natural Sciences|Nagoya University
Yanaka, Saeko
National Institutes of Natural Sciences|Nagoya City University
Uchiyama, Susumu
National Institutes of Natural Sciences|Osaka University
Kato, Koichi
National Institutes of Natural Sciences|Nagoya City University
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Content Type |
Journal Article
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Description | 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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Journal Title |
Scientific Reports
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ISSN | 20452322
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Publisher | Springer Nature
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Volume | 9
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Start Page | 11957
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Published Date | 2019-08-16
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Rights | This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
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language |
eng
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departments |
Bioscience and Bioindustry
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