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5. Production of Antigen-Binding Fragment against O , O -Diethyl Organophosphorus Pesticides and Molecular Dynamics Simulations of Antibody Recognition.

Author

Chen ZJ, Zhang X, Wang BF, Rao MF, Wang H, Lei HT, Liu H, Zhang Y, Sun YM, and Xu ZL

Subjects
Animals, Antibodies, Monoclonal genetics, Antibodies, Monoclonal immunology, Antibody Formation genetics, Enzyme-Linked Immunosorbent Assay methods, Humans, Immunoglobulin Fab Fragments genetics, Mice, Molecular Docking Simulation, Molecular Dynamics Simulation, Organophosphorus Compounds adverse effects, Organophosphorus Compounds immunology, Pesticides adverse effects, Pesticides isolation & purification, Recombinant Proteins immunology, Antibody Formation immunology, Immunoglobulin Fab Fragments immunology, Organophosphorus Compounds isolation & purification, Pesticides immunology
Abstract

Immunoassay for pesticides is an emerging analytical method since it is rapid, efficient, sensitive, and inexpensive. In this study, a recombinant antigen-binding fragment (Fab) against a broad set of O , O -diethyl organophosphorus pesticides (DOPs) was produced and characterized. The κ chain and Fd fragment were amplified via PCR and inserted into the vector pComb3XSS and the soluble Fab on phagemid pComb3XSS was induced by isopropyl β -d-thiogalactoside in E. coli TOP 10F’. SDS-PAGE, Western blotting, and indirect competitive ELISA results indicated that Fab maintained the good characteristics of the parental mAb. To better understand antibody recognition, the three-dimensional (3D) model of Fab was built via homologous modeling and the interaction between Fab and DOPs was studied via molecular docking and dynamics simulations. The model clearly explained the interaction manner of Fab and DOPs, and showed that the Arg-L96 and Arg-H52 were mainly responsible for antibody binding. This work provided a foundation for further mutagenesis of Fab to improve its characteristics.

Published
2018
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