Tyrosine Sulfation at Antibody Light Chain CDR-1 Increases Binding Affinity and Neutralization Potency to Interleukine-4

Tyrosine Sulfation at Antibody Light Chain CDR-1 Increases Binding Affinity and Neutralization Potency to Interleukine-4

Structure and function of therapeutic antibodies can be modulated by a variety of post-translational modifications (PTM). Tyrosine (Tyr) sulfation is a type of negatively charged PTM that occurs during protein trafficking through the Golgi. In this study, we discovered that an anti-interleukin (IL)-...

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Bibliographic Details
Main Authors: Aaron M. D’Antona, Julie M. Lee, Melvin Zhang, Clarence Friedman, Tao He, Lidia Mosyak, Eric Bennett, Laura Lin, Maddison Silverman, Funi Cometa, Caryl Meade, Tyler Hageman, Eric Sousa, Justin Cohen, Kimberly Marquette, Darren Ferguson, Xiaotian Zhong
Format: Article
Language:English
Published: MDPI AG 2024-02-01
Series:International Journal of Molecular Sciences
Subjects:
tyrosine sulfation
complementarity-determining region (CDR)
antigen-binding affinity
interleukine-4
cytokine signaling
Online Access:https://www.mdpi.com/1422-0067/25/3/1931

Internet

https://www.mdpi.com/1422-0067/25/3/1931

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