9KAT

Crystal structure of anti-sulfonylurea antibody scFv apo form

Summary for 9KAT

• Entry DOI: 10.2210/pdb9kat/pdb
• Descriptor: anti-sulfonylurea antibody scFv (2 entities in total)
• Functional Keywords: antibody, immune system
• Biological source: Mus musculus
• Total number of polymer chains: 2
• Total formula weight: 54999.38

Authors

Yu, X.T.,Gao, Y.G.,Lei, H.T. (deposition date: 2024-10-29, release date: 2025-04-16, Last modification date: 2025-04-30)

Primary citation

Yu, X.,Zhou, T.,Pan, K.,Fan, M.H.,Yan, X.,Huang, X.A.,Zhang, H.,Shen, X.,Xie, H.,Gao, Y.G.,Lei, H.
Structure Profiling of Broad-Specificity Immunoassays: Multitarget Recognition for Sulfonylurea Adulteration in Food.
J.Agric.Food Chem., 73:9348-9358, 2025

PubMed Abstract: The limited understanding of the broad-specific antibody recognition mechanism significantly hinders the development of immunoassays for simultaneously detecting illegal adulterants. Herein, a recombinant antisulfonylureas (SUs) single-chain variable fragment (scFv), which retained the properties of its parental monoclonal antibody, was successfully generated. X-ray crystallography, molecular docking, functional assays, and mutation validation were used to investigate the structure-function relationships underlying antibody-SUs binding. Our study revealed three key mechanisms for broad specificity: (1) the conformational adaptability of the scFv, which enabled various SUs to access the binding pocket; (2) the role of the Trp98 residue in CDR-L3 in modulating binding affinities among multiple SUs; and (3) the design of haptens with common structures and more rigid R substituents, which emerged as a promising strategy for generating broad-specific antibodies. This study provides a comprehensive analysis of the broad-specific recognition mechanism, offering valuable insights for rational hapten design and targeted antibody evolution to advance multitarget immunoassays.

PubMed: 40173361
DOI: 10.1021/acs.jafc.5c00655

Experimental method

X-RAY DIFFRACTION (1.51 Å)