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.
| Main Authors: | , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2020-12-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-20143-x |
| _version_ | 1818681630325211136 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-17T10:06:00Z |
| format | Article |
| id | doaj.art-731be2a1b0e94f0d9e6e6bb1c65b39da |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-17T10:06:00Z |
| publishDate | 2020-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-731be2a1b0e94f0d9e6e6bb1c65b39da2022-12-21T21:53:09ZengNature PortfolioNature Communications2041-17232020-12-0111111210.1038/s41467-020-20143-xBivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hingeHenry R. Maun0Rajesh Vij1Benjamin T. Walters2Ashley Morando3Janet K. Jackman4Ping Wu5Alberto Estevez6Xiaocheng Chen7Yvonne Franke8Michael T. Lipari9Mark S. Dennis10Daniel Kirchhofer11Claudio Ciferri12Kelly M. Loyet13Tangsheng Yi14Charles Eigenbrot15Robert A. Lazarus16James T. Koerber17Department of Early Discovery Biochemistry, Genentech, Inc.Department of Antibody Engineering, Genentech, Inc.Department of Biochemical and Cellular Pharmacology, Genentech, Inc.Department of Biochemical and Cellular Pharmacology, Genentech, Inc.Department of Immunology Discovery, Genentech, Inc.Department of Structural Biology, Genentech, Inc.Department of Structural Biology, Genentech, Inc.Department of Antibody Engineering, Genentech, Inc.Department of Biomolecular Resources, Genentech, Inc.Department of Early Discovery Biochemistry, Genentech, Inc.Department of Antibody Engineering, Genentech, Inc.Department of Early Discovery Biochemistry, Genentech, Inc.Department of Structural Biology, Genentech, Inc.Department of Biochemical and Cellular Pharmacology, Genentech, Inc.Department of Immunology Discovery, Genentech, Inc.Department of Structural Biology, Genentech, Inc.Department of Early Discovery Biochemistry, Genentech, Inc.Department of Antibody Engineering, Genentech, Inc.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.https://doi.org/10.1038/s41467-020-20143-x |
| spellingShingle | 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 Nature Communications |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41467-020-20143-x |
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