Antimetabolic effects of plant lectins and plant and fungal enzymes on the nymphal stages of two important rice pests, <i>Nilaparvata lugens</i> and <i>Nephotettix cinciteps</i>

Powell, Kevin; Gatehouse, A. M. R.; Hilder, Vaughan A.; Gatehouse, John A.

doi:10.1111/j.1570-7458.1993.tb00699.x

Cited by 170 publications

(122 citation statements)

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“…Recently, such a mechanism of GNA toxicity to BPH has been confirmed . In our studies, the expression of GNA in transgenic rice caused similar insecticidal effects to those of GNA fed to BPH and GLH in artificial diets (Powell et al, 1993), with decreased feeding as well as decreased insect survival (Figures 6 and 7). Marked decreases in the honeydew production of both BPH (80.08%) and GLH (69.06%) insects were observed when fed on T 2 homozygous plants ( Figure 6), thus suggesting the high feeding deterrent effect of GNA against both the insects.…”

Section: Discussionmentioning

confidence: 71%

“…Two major homopteran pests, rice brown planthopper (Nilaparvata lugens) and rice green leafhopper (Nephotettix virescens) cause severe physiological damage to the rice plant, as well as acting as vectors for rice tungro virus, grassy stunt virus, and ragged stunt virus (Mochida et al, 1979;Saxena and Khan, 1989). Earlier investigations (Powell et al, 1993) indicated that the snowdrop-lectin protein (GNA), which was isolated from the ornamental monocotyledonous plant, Galanthus nivalis (snowdrop), belonging to Amarillidaceae family, is toxic to sap-sucking insects of rice. Furthermore, it was reported that the snowdrop-lectin gene (gna), which is expressed in japonica rice (Rao et al, 1998) and wheat (Stoger et al, 1999), conferred resistance against rice brown planthopper and grain aphid, respectively.…”

Section: Among the Available Genetic Transformation Methodsmentioning

confidence: 99%

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Transgenic indica rice resistant to sap‐sucking insects

Nagadhara

Ramesh

Pasalu

et al. 2003

Plant Biotechnology Journal

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SummaryAgrobacterium-mediated genetic transformation has been optimized in indica rice susceptible to sap-sucking insects, viz., brown planthopper (BPH) and green leafhopper (GLH). Snowdrop lectin gene ( gna) from Galanthus nivalis, driven by phloem-specific rice-sucrose-synthase promoter, along with herbicide resistance gene (bar) driven by CaMV 35S promoter, was employed for genetic transformation. Embryogenic calli -after cocultivation with Agrobacterium strain LBA4404 harbouring Ti plasmid pSB111-bar-gnawere selected on the medium containing phosphinothricin. PCR and Southern blot analyses confirmed the stable integration of both the genes into genomes of transgenic (T 0 ) rice plants. Northern and Western blot analyses revealed the expression of gna in the transgenic plants. In the T 1 and T 2 generations, the gna and bar transgenes showed co-segregation at a ratio of 3 : 1. Plant progenies expressing gna, in T 1 and T 2 , exhibited substantial resistance against BPH and GLH pests. This is the first report dealing with transgenic indica rice exhibiting high resistance to both insects.

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Section: Discussionmentioning

confidence: 71%

Section: Among the Available Genetic Transformation Methodsmentioning

confidence: 99%

Transgenic indica rice resistant to sap‐sucking insects

Nagadhara

Ramesh

Pasalu

et al. 2003

Plant Biotechnology Journal

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“…Five third instar nymphs of N. lugens were refolded on the column by gradually removing the denaturant. removed from the host plant using a fine paintbrush to minimise The protein was eluted in 300 mM imidazole and diluted to physical damage, and placed in a plastic feeding chamber [24]. 100 µg/ml in 50 mM Tris/HCl pH 7.9.…”

Section: Resultsmentioning

confidence: 99%

Production and purification of active snowdrop lectin in Escherichia coli

Longstaff

Powell

Gatehouse

et al. 1998

European Journal of Biochemistry

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Recombinant snowdrop lectin was produced in Escherichia coli from a cDNA clone encoding mature Galanthus nivalis agglutinin. After induction with isopropylthio-β-D-galactoside, inclusion bodies from E. coli were solubilised and the G. nivalis agglutinin purified by metal-affinity chromatography using a carboxy-terminal hexahistidine tag. The protein was refolded on the metal-affinity column prior to elution. After purification, the recombinant G. nivalis agglutinin agglutinated rabbit erythrocytes to a dilution similar to that determined for 'native' lectin purified from snowdrop, and showed similar specific binding to mannose. The toxicity of the recombinant G. nivalis agglutinin towards rice brown planthopper (Nilaparvata lugens) was shown to be similar to that of 'native' G. nivalis agglutinin when incorporated into an artificial diet. The recombinant G. nivalis agglutinin is thus functionally similar to 'native' snowdrop lectin.Keywords : snowdrop (Galanthus nivalis); lectin ; bacterial expression system; recombinant protein; functional activity.Plant lectins constitute a heterogeneous group of proteins eration of Escherichia coli in the small intestine of rats when with different biochemical properties and carbohydrate-binding included as part of the diet [10]. specificities. They are widespread throughout the plant kingdom,In its natural state, the snowdrop lectin isolated from bulbs occurring in a number of plant species from all major taxonomic exists as a highly complex mixture of isoforms as evidenced by groupings. Lectins found in plants of the monocotyledonous isoelectric focussing [4]. Since snowdrop bulb tissue is rich in group are distinct from those of the dicotyledons and exhibit polysaccharides, which interfere with extraction processes, several unique properties. Snowdrop lectin (Galanthus nivalis young developing ovaries, which contain high concentrations of agglutinin) was first isolated from bulbs of the snowdrop G. lectin and are low in RNAse activity, were chosen as the starting nivalis L., and characterised as a tetrameric protein of 50 kDa material for nucleic acid extraction [11]. A cDNA library was composed of four identical subunits [1]. This lectin is unique in constructed from total poly(A)-rich RNA isolated from snowthat it recognizes A-D-mannose groups, in particular those link-drop ovaries and used to obtain five lectin clones [11], which ages made by Man(A1-3)Man units [2]; this exclusive specificity differed with respect to their nucleotide sequence and deduced for mannose is shared by members of the families Amaryllida-amino acid sequence. One of these clones, LECGNA2, was subceae [3] and Alliaceae [4] and distinguishes snowdrop lectin sequently used to produce constructs for transformation of the from the mannose/glucose-binding lectins of legumes such as G. nivalis agglutinin gene into plants [12Ϫ14]. jackbean (Canavalia ensiformis L. DC) and pea (Pisum sativum A number of plant lectins, including snowdrop lectin, have L.). Crystallographic studies have confirmed that G. n...

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“…The insecticidal activity of Man-binding lectins has been demonstrated against a spectrum of insects, both in artificial diets supplemented with the lectins (Powell et al, 1993;Fitches et al, 2001) and also when insects feed on natural and transgenic plants expressing lectins (Gatehouse et al, 1996;Nagadhara et al, 2004;Sadeghi et al, 2008). The snowdrop lectin, GNA, is toxic to brown planthopper (Nilaparvata lugens; Powell et al, 1998;Tang et al, 2001) and tomato moth (Lacanobia oleracea) larvae (Fitches et al, 1997;Gatehouse et al, 1997Gatehouse et al, , 1999 as well as to several aphid species (Hilder et al, 1995;Rahbé et al, 1995;Gatehouse et al, 1996;Sauvion et al, 1996).…”

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confidence: 99%

“…The insecticidal activity is attributed to lectin recognition of Man glycans in the digestive tracts of insects (Fitches et al, 2001;Majumder et al, 2004). Immunohistochemical studies show that these lectins bind to carbohydrate moieties of glycoproteins on epithelial cells lining the luminal surface of insect midguts, such as the binding of GNA in brown planthopper (Powell et al, 1993(Powell et al, , 1998 and concanavalin A in pea aphids (Acyrthosiphon pisum; Sauvion et al, 2004). An additional target is the peritrophic matrix lining the midgut region.…”

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confidence: 99%

Functional Characterization of HFR1, a High-MannoseN-Glycan-Specific Wheat Lectin Induced by Hessian Fly Larvae

et al. 2008

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We previously cloned and characterized a novel jacalin-like lectin gene from wheat (Triticum aestivum) plants that responds to infestation by Hessian fly (Mayetiola destructor) larvae, a major dipteran pest of this crop. The infested resistant plants accumulated higher levels of Hfr-1 (for Hessian fly-responsive gene 1) transcripts compared with uninfested or susceptible plants. Here, we characterize the soluble and active recombinant His 6 -HFR1 protein isolated from Escherichia coli. Functional characterization of the protein using hemagglutination assays revealed lectin activity. Glycan microarray-binding assays indicated strong affinity of His 6 -HFR1 to Mana1-6(Mana1-3)Man trisaccharide structures. Resistant wheat plants accumulated high levels of HFR1 at the larval feeding sites, as revealed by immunodetection, but the avirulent larvae were deterred from feeding and consumed only small amounts of the lectin. Behavioral studies revealed that avirulent Hessian fly larvae on resistant plants exhibited prolonged searching and writhing behaviors as they unsuccessfully attempted to establish feeding sites. During His 6 -HFR1 feeding bioassays, Drosophila melanogaster larvae experienced significant delays in growth and pupation, while percentage mortality increased with progressively higher concentrations of His 6 -HFR1 in the diet. Thus, HFR1 is an antinutrient to dipteran larvae and may play a significant role in deterring Hessian fly larvae from feeding on resistant wheat plants.

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Antimetabolic effects of plant lectins and plant and fungal enzymes on the nymphal stages of two important rice pests, Nilaparvata lugens and Nephotettix cinciteps

Cited by 170 publications

References 16 publications

Transgenic indica rice resistant to sap‐sucking insects

Transgenic indica rice resistant to sap‐sucking insects

Production and purification of active snowdrop lectin in Escherichia coli

Functional Characterization of HFR1, a High-MannoseN-Glycan-Specific Wheat Lectin Induced by Hessian Fly Larvae

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