Abstract
Bacteriophage expression systems offer promise for the development of novel antibody reagents applicable to the detection of microbial agents and their toxins in foods. Recombinant single chain variable region fragments (scFv) specific to either fumonisin B1 (FB1) or zearalenone were displayed on the surface of recombinant phage, or as soluble protein after infection of E. coli HB2151. Compared to polyclonal or monoclonal antibodies for FB1, the recombinant anti-FB1 scFv proteins were 10 to 100 times less sensitive in a competitive indirect enzyme linked immunosorbent assay (CI-ELISA). High affinity anti-zearalenone scFv phage were enriched through affinity selection in microtiter wells coated with zearalenone-ovalbumin conjugate. Sensitivity of the anti-zearalenone scFv phage displayed protein or soluble protein was similar to the parent monoclonal antibody (IC50 of 14 ng/ml vs 17 ng/ml), but exhibited higher cross reactivity with zearalenone analogs. Affinity selection via a competitive elution was necessary for the isolation of the variable regions of anti-zearalenone scFv with the desired affinity.KeywordsRecombinant AntibodyRecombinant PhageAffinity SelectionAntibody ReagentscFv ProteinThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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