Abstract

Anti-idiotype antibodies (Ab2) for fumonisin B1 (FmB1) were demonstrated in rabbits after immunization with purified monoclonal antibody (mAb1) against FmB1. Ab2 bound specifically to FmB1-mAb1. Indirect competitive ELISA revealed that the binding of to FmB1-ovalbumin (OVA) was inhibited by Ab2. Ab2 could also be used as FmB1-OVA surrogate in the ELISA for FmB1. In the FmB1-OVA-based ELISA, the concentrations causing 50% inhibition (ID50) of binding of mAb1 to FmB1-OVA by FmB1 and FmB2 were found to be 0.14 and 0.15 microgram/mL, respectively. In the Ab2-based ELISA, the ID50 values of binding of mAb1 to Ab2 by FmB1 and FmB2 were found to be 0.46 and 0.61 microgram/mL, respectively. A good correlation was found between the data obtained from the FmB1-OVA-based and the Ab2-based ELISA for the analysis of FmB1 in corn. Using the affinity-purified Ab2 Fab fragment as immunogen, polyclonal anti-Ab2 antibodies (Ab3) were generated in BALB/c mice. The Ab3 was found to have characteristics similar to those of original mAb1. The ID50 values of binding of Ab3 to FmB1-OVA by FmB1 and FmB2 were found to be 0.19 and 0.26 microgram/mL, respectively.

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