ArticleJournal of industrial microbiology & biotechnology2015
Expression of V(H)-linker-V(L) orientation-dependent single-chain Fv antibody fragment derived from hybridoma 2E6 against aflatoxin B1 in Escherichia coli.
Article in Journal of industrial microbiology & biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- Structural Homology Fails to Predict Secretion Efficiency inInternational journal of molecular sciences · 2025Article
- Generation of a highly specific recombinant full-length antibody for detecting ethirimol in fruit and environmental water.Journal of hazardous materials · 2024Article
- Development of a plant-produced recombinant monoclonal antibody against Δ-9-tetrahydrocannabinol (Δ9-THC) for immunoassay application.Biotechnology reports (Amsterdam, Netherlands) · 2022Article
- Camelization of a murine single-domain antibody against aflatoxin BMycotoxin research · 2022Article
- Designing and generating a single-chain fragment variable (scFv) antibody against IL2Rα (CD25): AnIranian journal of basic medical sciences · 2021Article
- Effects of variable domain orientation on anti-HER2 single-chain variable fragment antibody expressed in the Escherichia coli cytoplasm.Biotechnology progress · 2021Article
- Generation of single-chain Fv antibody fragments against Mu-2-related death-inducing gene in Escherichia coli.Molecular biology reports · 2019Article
- One-Step Ultrasensitive Bioluminescent Enzyme Immunoassay Based on Nanobody/Nanoluciferase Fusion for Detection of Aflatoxin BJournal of agricultural and food chemistry · 2019Article
- A novel anti-p21Ras scFv antibody reacting specifically with human tumour cell lines and primary tumour tissues.BMC cancer · 2016Article
- Synthetic approach to the generation of antibody diversity.BMB reports · 2015Review
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Authors and funding
5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Aflatoxin B1 (AFB1) is a toxic secondary metabolic product, which threatens human and animal health. Antibody is a key factor for immunoassay against toxic stuff like AFB1, and single-chain Fv antibody fragment (scFv) has become a popular format of genetically engineered antibody. In this study, four hybridoma cell lines against AFB1 were obtained, and then scFvs 2E6 derived from hybridoma cell line 2E6 were constructed in different V(H)/V(L) orientations. Subsequently, scFvs 2E6 were expressed in E. coli BL21(DE3) mainly in the form of inclusion body. SDS-PAGE, Western blot and ELISA were employed to characterize scFvs 2E6. The results revealed that the yield of inclusion body of scFvs 2E6 in either V(H)/V(L) orientation was similar; however, only the scFv in V(H)-linker-V(L) orientation showed anti-AFB1 bioactivity after refolding. The present study underscores the importance of choosing optimal V(H)/V(L) orientation for scFv construction, and scFv may be favorable for immunoassays in food industry.
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