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Abstract
Monoclonal antibodies were prepared against the fumonisins, a group of mycotoxins produced by the plant pathogen, Fusarium moniliforme. Splenic lymphocytes, from Balb/c mice immunized with fumonisin B1‐ovalbumin conjugate, were fused with SP2/O myeloma cells, and 14 hybridomas were selected. In a competitive enzyme‐linked immunosorbent assay, fumonisin B1‐bovine serum albumin and free fumonisin B1 (FB1) competed for the monoclonal antibody. The concentrations of FB1 required to inhibit 50% antibody binding (IC50) ranged from 300 to 670 ppb. Antibodies also cross‐reacted with fumonisins B2 and B3 (FB2, FB3), and the hydrolyzed backbone of fumonisin B1 (HB‐FB1). None of the 14 monoclonal antibodies recognized the sphingolipids, sphingosine and sphinganine, that are structurally similar to the backbone of the fumonisins. Three‐dimensional computer models of FB1, FB2 and FB3 show the amine backbone folding with the two esterified trimethyl‐propane‐1,2,3‐tricarboxylic acid side‐chains to form a cage into which...
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