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National Institute of Environmental Health Sciences

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Your Environment. Your Health.

Publication Detail

Title: Inactivation of the lipoxygenase ZmLOX3 increases susceptibility of maize to Aspergillus spp.

Authors: Gao, Xiquan; Brodhagen, Marion; Isakeit, Tom; Brown, Sigal Horowitz; Göbel, Cornelia; Betran, Javier; Feussner, Ivo; Keller, Nancy P; Kolomiets, Michael V

Published In Mol Plant Microbe Interact, (2009 Feb)

Abstract: Plant and fungal lipoxygenases (LOX) catalyze the oxidation of polyunsaturated fatty acids, creating fatty-acid hydroperoxides (oxylipins). Fungal oxylipins are required for normal fungal development and secondary metabolism, and plant host-derived oxylipins interfere with these processes in fungi, presumably by signal mimicry. The maize LOX gene ZmLOX3 has been implicated previously in seed-Aspergillus interactions, so we tested the interactions of a mutant maize line (lox3-4, in which ZmLOX3 is disrupted) with the mycotoxigenic seed-infecting fungi Aspergillus flavus and Aspergillus nidulans. The lox3-4 mutant was more susceptible than wild-type maize to both Aspergillus species. All strains of A. flavus and A. nidulans produced more conidia and aflatoxin (or the precursor sterigmatocystin) on lox3-4 kernels than on wild-type kernels, in vitro and under field conditions. Although oxylipins did not differ detectably between A. flavus-infected kernels of the lox3-4 and wild-type (WT) maize, oxylipin precursors (free fatty acids) and a downstream metabolite (jasmonic acid) accumulated to greater levels in lox3-4 than in WT kernels. The increased resistance of the lox3-4 mutant to other fungal pathogens (Fusarium, Colletotrichum, Cochliobolus, and Exserohilum spp.) is in sharp contrast to results described herein for Aspergillus spp., suggesting that outcomes of LOX-governed host-pathogen interactions are pathogen-specific.

PubMed ID: 19132874 Exiting the NIEHS site

MeSH Terms: Aflatoxins/biosynthesis; Aspergillus/growth & development; Aspergillus/physiology*; Cyclopentanes/analysis; Disease Susceptibility; Enzyme Activation; Fatty Acids/analysis; Lipid Metabolism; Lipoxygenase/genetics*; Lipoxygenase/metabolism; Mutation/genetics*; Oxylipins/analysis; Oxylipins/metabolism; Phenotype; Plant Diseases/microbiology; Plant Proteins/genetics*; Plant Proteins/metabolism; Spores, Fungal/enzymology; Sterigmatocystin/biosynthesis; Zea mays/enzymology*; Zea mays/microbiology*

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