Evidence map›Paper›PMID 40670938›Full record

ArticleBMC biotechnology2025

An anti-idiotypic single domain antibody as Cry2Aa toxin mimotope and analysis of its binding region through molecular docking.

Manman Lin, Guangjie Han, Chuanming Li, Lixin Huang, Qin Liu, Nan Zhang, Yang Xia, Yurong Lu, Xianjin Liu, Yuan Liu and 2 more

Abstract read
In one paragraph

Article in BMC biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

12 authors.

Manman LinNational Agricultural Experimental Station for Agricultural Microbiology in Yangzhou, Jiangsu Lixiahe District Institute of Agricultural Sciences, Yangzhou, 225007, China.
Guangjie HanNational Agricultural Experimental Station for Agricultural Microbiology in Yangzhou, Jiangsu Lixiahe District Institute of Agricultural Sciences, Yangzhou, 225007, China.
Chuanming LiNational Agricultural Experimental Station for Agricultural Microbiology in Yangzhou, Jiangsu Lixiahe District Institute of Agricultural Sciences, Yangzhou, 225007, China.
Lixin HuangNational Agricultural Experimental Station for Agricultural Microbiology in Yangzhou, Jiangsu Lixiahe District Institute of Agricultural Sciences, Yangzhou, 225007, China.
Qin LiuNational Agricultural Experimental Station for Agricultural Microbiology in Yangzhou, Jiangsu Lixiahe District Institute of Agricultural Sciences, Yangzhou, 225007, China.
Nan ZhangNational Agricultural Experimental Station for Agricultural Microbiology in Yangzhou, Jiangsu Lixiahe District Institute of Agricultural Sciences, Yangzhou, 225007, China.
Yang XiaNational Agricultural Experimental Station for Agricultural Microbiology in Yangzhou, Jiangsu Lixiahe District Institute of Agricultural Sciences, Yangzhou, 225007, China.
Yurong LuNational Agricultural Experimental Station for Agricultural Microbiology in Yangzhou, Jiangsu Lixiahe District Institute of Agricultural Sciences, Yangzhou, 225007, China.
Xianjin LiuJiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Institute of Food Safety and Nutrition, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China.
Yuan LiuJiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Institute of Food Safety and Nutrition, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China. 20050006@jaas.ac.cn.
Jian XuNational Agricultural Experimental Station for Agricultural Microbiology in Yangzhou, Jiangsu Lixiahe District Institute of Agricultural Sciences, Yangzhou, 225007, China. bio-xj@163.com.
Johnson LinSchool of Life Sciences, Discipline of Microbiology, College of Agriculture, Engineering and Science, University of KwaZulu-Natal, Westville Campus, Durban, 4000, South Africa.

Funding

Jiangsu Agricultural Science and Technology Innovation Fund CX(24)3011Key Laboratory Project of Yangzhou YZ2023244National Agricultural Basic Long-Term Scientific and Technological Work NAES069AM04National Key Research and Development Program of China 2023YFE0109400National Natural Science Foundation of China 32372539
6 · The paper itself

Abstract

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')

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.

Indexed as

Antibodies, Anti-IdiotypicBacterial ProteinsEndotoxinsHemolysin ProteinsSingle-Domain AntibodiesAmino Acid SequenceAnimalsBacillus thuringiensis ToxinsBinding SitesEpitopesMolecular Docking SimulationMolecular MimicryPeptide LibraryProtein BindingAntibodies, Anti-IdiotypicBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsEpitopesHemolysin Proteinsinsecticidal crystal protein, Bacillus ThuringiensisPeptide LibrarySingle-Domain AntibodiesAnti-idiotypic antibodyCry2Aa toxinEpitopesMimotopeMolecular dockingSingle-domain antibody

Identifiers

PMID40670938
PMCPMC12269107

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.