Abstract
Concanavalin A (ConA), a legume lectin, has been drawing increasing attention in recent years concerning its toxicity against insects and its potential application in pest management. In an attempt to evaluate the effect of ConA on potato psyllid (Bactericera cockerelli), an economically important pest of solanaceous crops, the effect of ConA on potato psyllid survival, psyllid gut nuclear morphology, and expression of psyllid caspase genes were evaluated. Our results determined that artificial diet-feeding assays using ConA had deleterious effects on potato psyllids, resulting in significant psyllid mortality following ingestion. We also found that an apoptotic response was induced by ConA in psyllid midgut cells, which was demonstrated by the DNA fragmentation and abnormal nuclear architecture in the midgut cells. Following ConA ingestion, there was also upregulation of caspase genes in the psyllid midguts. Therefore, a key mechanism behind ConA toxicity towards potato psyllid probably involves the induction of apoptosis in midgut cells. This study could provide a better understanding of the mechanisms underlying ConA toxicity in insects and be a stepping stone towards the development of new psyllid control strategies based on plant lectins.
Highlights
Lectins are a class of plant proteins with at least one non-catalytic domain that can and reversibly bind to carbohydrates without altering the covalent structure of the recognized glycosyl ligands [1,2]
Days of feeding on the Concanavalin A (ConA)-containing diets, the number of dead LsoA-infected psyllids was significantly higher than Liberibacter solanacearum’ (Lso)-free psyllids (F2,6 = 5.182, p < 0.05), there was no significant difference in the survival rate among Lso-free and Lso-infected psyllids feeding on ConA after three days (p > 0.05)
The results showed that ConA significantly increased psyllid mortality when compared to the control diets lacking ConA whether psyllids were Lso-free, LsoA, or LsoB-infected (Figure 1b)
Summary
Lectins are a class of plant proteins with at least one non-catalytic domain that can and reversibly bind to carbohydrates without altering the covalent structure of the recognized glycosyl ligands [1,2]. Lectins show the greatest potential for exploitation in transgenic-based pest control strategies [5]. These proteins could be important as control agents for hemipteran pests because these insects are not susceptible to Bacillus thuringiensis (Bt) toxins [6,7]. Concanavalin A (ConA), a lectin from Canavalia ensiformis, is one of the most extensively investigated members of the lectin family of plant proteins [8]. ConA has previously been demonstrated to be detrimental to multiple pest species, such as the tomato moth, the cotton bollworm/legume pod borer, as well as several aphid species [9,10,11,12]
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