ArticleApplied and environmental microbiology1997
Molecular cloning, expression, and characterization of a functional single-chain Fv antibody to the mycotoxin zearalenone.
Article in Applied and environmental microbiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 67 citations in OpenAlex.
- Mimotopes for Mycotoxins Diagnosis Based on Random Peptides or Recombinant Antibodies from Phage Library.Molecules (Basel, Switzerland) · 2021Review
- Article
- The reduced form of the antibody CH2 domain.Protein science : a publication of the Protein Society · 2021Article
- Engineered resistance to Nosema bombycis by in vitro expression of a single-chain antibody in Sf9-III cells.PloS one · 2018Article
- Sensitive giant magnetoresistive-based immunoassay for multiplex mycotoxin detection.Biosensors & bioelectronics · 2010Article
- Modification of the ionizing radiation response in living cells by an scFv against the DNA-dependent protein kinase.Nucleic acids research · 2003Article
- Expression of a functional antizearalenone single-chain Fv antibody in transgenic Arabidopsis plants.Applied and environmental microbiology · 2000Article
- Identification of mimotope peptides which bind to the mycotoxin deoxynivalenol-specific monoclonal antibody.Applied and environmental microbiology · 1999Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heavy-chain and kappa light-chain variable region genes of an antizearalenone hybridoma cell line (2G3-6E3-2E2) were isolated by PCR and joined by a DNA linker encoding peptide (Gly4Ser)3 as a single-chain Fv (scFv) DNA fragment. The scFv DNA fragment was cloned into a phagemid (pCANTAB5E) and expressed as a fusion protein with E tag and phage M13 p3 in Escherichia coli TG1. In the presence of helper phage M13K07, the scFv fusion protein was displayed on the surfaces of recombinant phages. High-affinity scFv phages were enriched through affinity selection in microtiter wells coated with zearalenone-ovalbumin conjugate. The selected recombinant phages were used to infect E. coli HB2151 for the production of soluble scFv antibodies. One selected clone (pQY1.5) in HB2151 secreted a soluble scFv antibody (QY1.5) with a high zearalenone-binding affinity (concentration required for 50% inhibition of binding, 14 ng/ml), similar to that of parent monoclonal antibody in a competitive indirect enzyme-linked immunosorbent assay. However, scFv QY1.5 exhibited higher cross-reactivity with zearalenone analogs and had greater sensitivity to methanol destabilization than the parent monoclonal antibody did. Nucleotide sequence analyses revealed that the light-chain portion of scFv QY1.5 had a nucleotide sequence identity of 97% to a mouse germ line gene VK23.32 in mouse kappa light-chain variable region subgroup V, whereas the heavy-chain nucleotide sequence was classified as mouse heavy-chain subgroup III (D) but without any closely related members having highly homologous complementarity-determining region sequences. The potential of soluble scFv QY1.5 for routine screening of zearalenone and its analogs was demonstrated with zearalenone-spiked corn extracts.
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