A monoclonal antibody was prepared against deoxynivalenol (DON, vomitoxin), a trichothecene mycotoxin occurring in grain contaminated with Gibberella zeae (anamorph = Fusarium graminearum), and incorporated into competitive direct and indirect enzyme-linked immunosorbent assays (ELISAs). DON antibodies were secreted by hybridomas derived from mice inoculated with DON conjugated to bovine serum albumin. Conjugation of DON to carrier proteins was facilitated by conversion of DON to 3-O-hemisuccinyl-DON after protection of two of the three available hydroxyls with a cyclic boronate ester. DON was detectable at 10-250 ng/assay (0.2-5.0 µg/mL) for direct ELISA and 10-150 ng/assay (0.2-2.0 µg/raL) for indirect ELISA. The monoclonal antibody cross-reacts with 3-acetyl-DON, 3-Ohemisuccinyl-DON, DON, 12,13-deepoxy-DON, nivalenol, and fusarenone X (in order of decreasing affinity) but has low affinity for 15-acetyl-DON and T-2 toxin. Deoxynivalenol (DON, vomitoxin) is one of the sesquiterpene mycotoxins classified as 12,13-epoxytrichothecenes (Mirocha et al, 1977). It occurs naturally in infected corn (Hart et al., 1982;Mirocha et al., 1976), small grains (Hart and Braselton, 1983; Neish and Cohen, require little sample preparation, are rapid and relatively simple to execute, yet are sensitive. In addition, enzyme immunoassays lack the health hazards associated with radioimmunoassays. Monoclonal antibodies have important advantages over polyclonal antibodies. They may be extremely specific, even if the immunizing antigen was not pure, and offer a theoretically unlimited supply of homo-
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