Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge
β-tryptases are responsible for most of the proteolytic activity during mast cell activation. Here, the authors develop β-tryptase-inhibiting antibodies and provide structural and biochemical evidence that the bivalency of the antibodies is a prerequisite for their inhibitory activity.
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Nature Portfolio
2020
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oai:doaj.org-article:731be2a1b0e94f0d9e6e6bb1c65b39da2021-12-02T10:48:19ZBivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge10.1038/s41467-020-20143-x2041-1723https://doaj.org/article/731be2a1b0e94f0d9e6e6bb1c65b39da2020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20143-xhttps://doaj.org/toc/2041-1723β-tryptases are responsible for most of the proteolytic activity during mast cell activation. Here, the authors develop β-tryptase-inhibiting antibodies and provide structural and biochemical evidence that the bivalency of the antibodies is a prerequisite for their inhibitory activity.Henry R. MaunRajesh VijBenjamin T. WaltersAshley MorandoJanet K. JackmanPing WuAlberto EstevezXiaocheng ChenYvonne FrankeMichael T. LipariMark S. DennisDaniel KirchhoferClaudio CiferriKelly M. LoyetTangsheng YiCharles EigenbrotRobert A. LazarusJames T. KoerberNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q Henry R. Maun Rajesh Vij Benjamin T. Walters Ashley Morando Janet K. Jackman Ping Wu Alberto Estevez Xiaocheng Chen Yvonne Franke Michael T. Lipari Mark S. Dennis Daniel Kirchhofer Claudio Ciferri Kelly M. Loyet Tangsheng Yi Charles Eigenbrot Robert A. Lazarus James T. Koerber Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge |
| description |
β-tryptases are responsible for most of the proteolytic activity during mast cell activation. Here, the authors develop β-tryptase-inhibiting antibodies and provide structural and biochemical evidence that the bivalency of the antibodies is a prerequisite for their inhibitory activity. |
| format |
article |
| author |
Henry R. Maun Rajesh Vij Benjamin T. Walters Ashley Morando Janet K. Jackman Ping Wu Alberto Estevez Xiaocheng Chen Yvonne Franke Michael T. Lipari Mark S. Dennis Daniel Kirchhofer Claudio Ciferri Kelly M. Loyet Tangsheng Yi Charles Eigenbrot Robert A. Lazarus James T. Koerber |
| author_facet |
Henry R. Maun Rajesh Vij Benjamin T. Walters Ashley Morando Janet K. Jackman Ping Wu Alberto Estevez Xiaocheng Chen Yvonne Franke Michael T. Lipari Mark S. Dennis Daniel Kirchhofer Claudio Ciferri Kelly M. Loyet Tangsheng Yi Charles Eigenbrot Robert A. Lazarus James T. Koerber |
| author_sort |
Henry R. Maun |
| title |
Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge |
| title_short |
Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge |
| title_full |
Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge |
| title_fullStr |
Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge |
| title_full_unstemmed |
Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge |
| title_sort |
bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the igg hinge |
| publisher |
Nature Portfolio |
| publishDate |
2020 |
| url |
https://doaj.org/article/731be2a1b0e94f0d9e6e6bb1c65b39da |
| work_keys_str_mv |
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| _version_ |
1718396655266430976 |