An anti-idiotypic single domain antibody as Cry2Aa toxin mimotope and analysis of its binding region through molecular docking
文献类型： 外文期刊
作者： Lin, Manman 1 ; Han, Guangjie 1 ; Li, Chuanming 1 ; Huang, Lixin 1 ; Liu, Qin 1 ; Zhang, Nan 1 ; Xia, Yang 1 ; Lu, Yurong 1 ; Liu, Xianjin 2 ; Liu, Yuan 2 ; Xu, Jian 1 ; Lin, Johnson 3 ;
作者机构： 1.Jiangsu Lixiahe Dist Inst Agr Sci, Natl Agr Expt Stn Agr Microbiol Yangzhou, Yangzhou 225007, Peoples R China
2.Jiangsu Acad Agr Sci, Inst Food Safety & Nutr, Jiangsu Key Lab Food Qual & Safety, State Key Lab Cultivat Base,Minist Sci & Technol, Nanjing 210014, Peoples R China
3.Univ KwaZulu Natal, Coll Agr Engn & Sci, Sch Life Sci, Discipline Microbiol, Westville Campus, ZA-4000 Durban, South Africa
关键词： Cry2Aa toxin; Anti-idiotypic antibody; Single-domain antibody; Epitopes; Mimotope; Molecular docking
期刊名称：BMC BIOTECHNOLOGY （ 影响因子：3.4； 五年影响因子：3.6 ）
ISSN：
年卷期： 2025 年 25 卷 1 期
页码：
收录情况： SCI
摘要： BackgroundAnti-idiotypic antibodies have garnered significant attention in biotechnology and immunology due to their unique ability to mimic specific epitopes on target antigens, thereby serving as functional analogues. This property makes them valuable tools for various applications. In this study, we aimed to isolate an anti-idiotypic single domain antibody against Cry2Aa from a naive phage-display library and investigate its structural and functional mimicry of the Cry2Aa toxin.ResultsAn anti-idiotypic single domain antibody (sdAb) specific for the Cry2Aa toxin was successfully isolated from a naive phage-display library. Sequence analysis revealed a 57.1% identity between the epitopes on Cry2Aa mimicked by the sdAb and Cry2Aa. The sdAb could compete with Cry2Aa toxin for binding to anti-Cry2Aa F(ab')2 fragments and potential Cry2Aa receptors, including aminopeptidase N5 (APN5), vacuolar-type proton ATPase subunit A (V-ATPase A), and toxin-binding region (CR9-CR11) of cadherin-like protein (Cad-TBR) from Plutella xylostella. Molecular docking simulations indicated that the complementarity determining regions 2 (CDR2) and CDR3 of the antibody played critical roles in binding to these receptors and alanine mutant binding studies also proved that CDR2 and CDR3 played critical roles in receptor binding. These results indicated that the Cry2Aa anti-idiotypic sdAb has the potential to characterize a similar pattern of molecular interactions as Cry2Aa toxin.ConclusionsThe findings from this study indicate that the isolated Cry2Aa anti-idiotypic sdAb mimics the molecular interaction pattern of the Cry2Aa toxin with its midgut receptors. The anti-idiotypic sdAb offers new potential for developing novel insect control strategies.
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