Tryptamine-induced resistance in tryptophan decarboxylase transgenic poplar and tobacco plants against their specific herbivores.
The presence of amines and their derivatives in plant tissues is known to influence insect feeding and reproduction. The enzyme tryptophan decarboxylase (TDC) catalyzes the decarboxylation of tryptophan to tryptamine, which is both a bioactive amine and a precursor of other indole derivatives. Transgenic poplar and tobacco plants ectopically expressing TDC1 accumulated elevated levels of tryptamine without affecting plant growth and development. This accumulation was consistently associated with adverse effects on feeding behavior and physiology of Malacosoma disstria Hub. (forest tent caterpillar, FTC) and Manduca sexta L. (tobacco hornworm, THW). Behavior studies with FTC and THW larvae showed that acceptability of the leaf tissue to larvae was inversely related to foliar tryptamine levels. Physiological studies with FTC and THW larvae showed that consumption of leaf tissue from the transgenic lines is deleterious to larvae growth, apparently due to a postingestive mechanism. Thus, ectopic expression of TDC1 can allow sufficient tryptamine to accumulate in poplar and tobacco leaf tissue to suppress significantly the growth of insect pests that normally feed on these plants.
Gill
Rishi I S
RI
UBC Biotechnology Laboratory and Faculty of Agricultural Sciences, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4.
Ellis
Brian E
BE
Isman
Murray B
MB
D000818:Animals; D001142:Aromatic-L-Amino-Acid Decarboxylases / Q000494:pharmacology*; D005247:Feeding Behavior; D005786:Gene Expression Regulation; D007300:Insect Control; D007814:Larva / Q000254:growth & development; D007915:Lepidoptera; D018515:Plant Leaves / Q000737:chemistry; D010945:Plants, Edible; D030821:Plants, Genetically Modified; D032107:Populus / Q000235:genetics*; D014026:Nicotiana / Q000235:genetics*; D014363:Tryptamines / Q000494:pharmacology*
D014363:Tryptamines; C030820:tryptamine; D001142:Aromatic-L-Amino-Acid Decarboxylases