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Culmorin inhibits detoxification of the mycotoxin deoxynivalenol by plant UDP-glucosyltransferases

Title: Culmorin inhibits detoxification of the mycotoxin deoxynivalenol by plant UDP-glucosyltransferases
Authors: Michlmayr, Herbert; Wiesenberger, Gerlinde; Rehak, Katrin; Sopel, Marta; Funtak, Kristina; Malachová, Alexandra; Fruhmann, Philipp; Weber, Julia; Dufresne, Marie; Krska, Rudolf; Berthiller, Franz; Adam, Gerhard
Source: Journal of Experimental Botany ; ISSN 0022-0957 1460-2431
Publisher Information: Oxford University Press (OUP)
Publication Year: 2026
Description: The Fusarium metabolite culmorin (CUL) frequently co-occurs with the mycotoxin deoxynivalenol (DON) on cereals. While DON is recognized as a major Fusarium virulence factor on plants, the function of CUL is still unclear. Herein, we show that CUL-deficient F. graminearum mutants created by CLM1 deletion are less aggressive on wheat than the wild-type, accompanied by increased DON-3-glucoside/DON ratios in infected wheat ears. In root elongation assays with wheat and Brachypodium distachyon, CUL had no effect alone but significantly increased the toxicity of DON. Analysis of DON/CUL-treated roots further indicated that both wheat and B. distachyon are able to glucosylate CUL and that its presence impedes DON-glucosylation in both species. We identified two B. distachyon UDP-glucosyltransferases (UGT) able to glucosylate CUL and further investigated the effect of CUL on the kinetics of validated DON-glucosylating plant UGTs (BdUGT5g03300, HvUGT13248, OsUGT79). This suggested that CUL inhibits DON-glucosylation either by serving as competitive substrate with DON or by unproductive binding. Especially BdUGT5g03300 was strongly inhibited by CUL and even its glucosides. Our results indicate that CUL contributes to Fusarium virulence by weakening plant-defences related to UGT-catalysed DON-detoxification. As even CUL-glucosides are potentially inhibitory to UGTs, this implies a complex synergy of CUL with DON.
Document Type: article in journal/newspaper
Language: English
DOI: 10.1093/jxb/erag158
DOI: 10.1093/jxb/erag158/67631392/erag158.pdf
Availability: https://doi.org/10.1093/jxb/erag158; https://academic.oup.com/jxb/advance-article-pdf/doi/10.1093/jxb/erag158/67631392/erag158.pdf
Rights: https://creativecommons.org/licenses/by/4.0/
Accession Number: edsbas.CC4657C4
Database: BASE