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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Patapoff, Thomas W. Lee, Chingwei V. Walters, Benjamin T. Janakiraman, Vasantharajan Fuh, Germaine Stinson, Jeremy Koenig, Patrick |
| Description | Author Affiliation: Koenig P ( Department of Antibody Engineering, Genentech Research and Early Development, Genentech, Inc., South San Francisco, CA 94080); Lee CV ( Department of Antibody Engineering, Genentech Research and Early Development, Genentech, Inc., South San Francisco, CA 94080.); Walters BT ( Department of Early-Stage Pharmaceutical Development, Pharma Technical Development, Genentech, Inc., South San Francisco, CA 94080.); Janakiraman V ( Department of Molecular Biology, Genentech Research and Early Development, Genentech, Inc., South San Francisco, CA 94080.); Stinson J ( Department of Molecular Biology, Genentech Research and Early Development, Genentech, Inc., South San Francisco, CA 94080.); Patapoff TW ( Department of Early-Stage Pharmaceutical Development, Pharma Technical Development, Genentech, Inc., South San Francisco, CA 94080.); Fuh G ( Department of Antibody Engineering, Genentech Research and Early Development, Genentech, Inc., South San Francisco, CA 94080); |
| Abstract | Somatic mutations within the antibody variable domains are critical to the immense capacity of the immune repertoire. Here, via a deep mutational scan, we dissect how mutations at all positions of the variable domains of a high-affinity anti-VEGF antibody G6.31 impact its antigen-binding function. The resulting mutational landscape demonstrates that large portions of antibody variable domain positions are open to mutation, and that beneficial mutations can be found throughout the variable domains. We determine the role of one antigen-distal light chain position 83, demonstrating that mutation at this site optimizes both antigen affinity and thermostability by modulating the interdomain conformational dynamics of the antigen-binding fragment. Furthermore, by analyzing a large number of human antibody sequences and structures, we demonstrate that somatic mutations occur frequently at position 83, with corresponding domain conformations observed for G6.31. Therefore, the modulation of interdomain dynamics represents an important mechanism during antibody maturation in vivo. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 4 |
| Volume Number | 114 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2017-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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