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Cross-reactivity of commercial and non-commercial deoxynivalenol-antibodies to emerging trichothecenes and common deoxynivalenol-derivatives

in World Mycotoxin Journal
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N.T. Nguyen Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, (BOKU), Konrad Lorenz Str. 24, 3430 Tulln, Austria.

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E. Varga Department of Agrobiotechnology (IFA-Tulln), Center for Analytical Chemistry, BOKU, Konrad Lorenz Str. 20, 3430 Tulln, Austria.

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C. Maragos Mycotoxin Prevention and Applied Microbiology Research Unit, USDA, ARS National Center for Agricultural Utilization Research, 1815 N. University St., Peoria, IL 61604, USA.

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S. Baumgartner Department of Agrobiotechnology (IFA-Tulln), Center for Analytical Chemistry, BOKU, Konrad Lorenz Str. 20, 3430 Tulln, Austria.

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G. Adam Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, (BOKU), Konrad Lorenz Str. 24, 3430 Tulln, Austria.

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F. Berthiller Department of Agrobiotechnology (IFA-Tulln), Center for Analytical Chemistry, BOKU, Konrad Lorenz Str. 20, 3430 Tulln, Austria.

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Immunoassay based techniques are an important and fast option for the detection and quantification of mycotoxins. They are frequently used as on-site screening tools in grain elevators, storage and production facilities. However, accurate quantification may be hampered by the co-recognition of structurally related metabolites by the used antibodies. Therefore, it is crucial to assess their cross-reactivity to avoid misinterpretation of the results. Several immunoassays for the determination of deoxynivalenol (DON) are commercially available. Recently, novel trichothecene mycotoxins with structures similar to DON, the NX-toxins (NX-2, NX-3 and NX-4), were discovered, which can potentially co-occur with DON in cereals. So far, no data about the cross-reactivity of those toxins with DON-antibodies are available. The aim of this study was to assess the cross-reactivities of NX-toxins and some other DON-related metabolites with DON-antibodies in buffer solutions. Six commercially available enzyme-linked immunosorbent assays (ELISAs) and two previously developed DON-antibodies (Mab#1 and Mab#22) were tested. Cross-reactivity with NX-metabolites was not observed for any of the ELISA-kits nor Mab#22, whereas Mab#1 reacted moderately against NX-3 and NX-4 (cross-reactivity based on a molar basis of 14 and 30%, respectively). Modifications at position C-3 (3-acetyl-DON and DON-3-glucoside) led to moderate or high cross-reactivity with Mab#22 and the commercial ELISA-kits, whereas these compounds were not recognised by Mab#1. Similar to NX-metabolites, 15-acetyl-DON interacted only weakly with Mab#22 and the commercial ELISA-kits, but strongly with Mab#1. The results demonstrate the importance of proper antibody characterisation. If NX-metabolites prove to be widely distributed and reach significant levels, the development of specific antibodies targeting these novel metabolites might become necessary.

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