| Plants have evolved
multiple mechanisms to defend themselves against herbivorous
insects. One technique they use is to manufacture and store
distasteful or toxic compounds in their leaves so that
caterpillars and other insects find that one bite is more than
enough, says Dan Kliebenstein, from the University of
California at Davis. Brassicas, which include broccoli,
cabbage, Brussels sprouts and
Arabidopsis thaliana, make compounds called
glucosinolates for this purpose. "All the flavors you hated to
eat as a child are glucosinolates," said Kliebenstein. For
humans, a slightly bitter taste is the worst of the
glucosinolates - and, in fact, these compounds are the ones
thought to have cancer fighting activity - but for small
insects who want to make their whole meal on raw
Arabidopsis, the problem can be much more significant.
The plant makes both a family of compounds called
glucosinolates and an enzyme called myrosinase. A healthy leaf
stores the two components in separate compartments. However,
when a caterpillar or other herbivorous insect takes a bite
out of the leaf, cell walls and compartments are broken down,
allowing the enzyme and glucosinolates to come into contact,
at which time the enzyme converts the bitter-tasting compound
into a toxic one.
Of course, over evolution some pests have found ways to get
around the problem. When Kliebenstein tested a pest who feeds
on a wide range of plants and is, therefore, categorized as a
generalist, he found that the caterpillars were sensitive to
the gluocsinolates. However, when he tested a specialist pest
that has evolved to feed almost exclusively on brassicas, he
found that, across the board, they were resistant to the toxic
effects of the glucosinolates.
So just how does a specialist pest, like
Plutella xylostella, avoid the toxin? To get an idea of
how the caterpillar was metabolizing the glucosinolates,
Kliebenstein and his colleagues collected the insect's feces,
dissolved it in water and analyzed it with high pressure
liquid chromatography (HPLC). Interestingly, the team found
that the glucosinolates were passing through the animal
relatively unchanged, as if the plant didn't even have the
myrosinase enzyme at all.
The researchers subsequently found that one of the major
proteins in the caterpillar's spit is an enzyme that removes a
sulfur group from the glucosinolates. Without this sulfur
group, the plant's own enzyme, myrosinase, doesn't recognize
the glucosinolate and therefore can't convert it to a toxic
compound, leaving the pest free to chew away at the now
defenseless plant.
"This is a nice bit of work," said Neal Gutterson, who
works on functional genomics in
Arabidopsis at Mendel Biotechnology, Inc. in Hayward,
California, "especially the part about how the specialist
detoxifies the compound."
Joseph Anderson, from the USDA/ARS Crop Production and Pest
Control Research Unit at Purdue University in West Lafayette,
Indiana, told BioMedNet News that Kliebenstein's work on
glucosinolates in
Arabidopsis is "quite applicable to other plant
systems." Because many plants use secondary metabolites, like
glucosinolates, what scientists learn in this model system
will be generally transferable to other plants - and their
pests. |