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- W2058779788 abstract "Abstract The activity of kievitone hydratase (KHase)—the enzyme catalysing detoxification of the phytoalexin, kievitone, to kievitone hydrate (KH)—in extracts of Fusarium solani f. sp. phaseoli -infected hypocotyls of Phaseolus vulgaris increased for several days and reached a peak at 5 days after inoculation. Several variants of the virulent isolate of F. solani f. sp. phaseoli were obtained, either following exposure of the fungus to the mutagenic chemical, N-methyl-N′-nitro-N-nitrosoguanidine, or by making transfers from naturally occurring sectors in agar cultures. These variants were monitored for pathogenicity to bean, sensitivity to kievitone and ability to cause clearing of an opaque, kievitone-amended, modified Fries agar—an assay which indicated KHase activity. All variants with reduced KHase activity were more sensitive to kievitone and were less pathogenic to bean than the virulent strain from which they were derived. No virulent isolate that lacked KHase was found. The presence of KHase in Fusarium -infected bean tissues soon after inoculation, and for several days thereafter, as well as the association between lowered KHase activity and reduced virulence, suggest that this enzyme plays a role in the development of the fungus in its host's tissues. Furthermore, these results are consistent with detoxification of the isoflavonoid, kievitone, by F. solani f. sp. phaseoli being important to the pathogenic behavior of this fungus." @default.
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- W2058779788 date "1984-09-01" @default.
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- W2058779788 title "Association between lowered kievitone hydratase activity and reduced virulence to bean in variants of Fusarium solani f. sp. phaseoli" @default.
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- W2058779788 doi "https://doi.org/10.1016/0048-4059(84)90052-3" @default.
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