Expression of snowdrop lectin in transgenic tobacco plants results in added protection against aphids

Hilder, Vaughan A.; Powell, Kevin; Gatehouse, Angharad M. R.; Gatehouse, John A.; Gatehouse, Laurence N.; She, Ying; Hamilton, W. D.; Merryweather, A.; Newell, C. A.; Timans, J. C.; Peumans, Willy J.; Damme, Els J.M. Van; Boulter, D.

doi:10.1007/bf01976497

Cited by 239 publications

(138 citation statements)

References 21 publications

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“…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). Concanavalin A (lectin from Canavalia ensiformis) shows significant antimetabolic activity toward third-instar nymphs of taro planthopper (Tarophagous proserpina; Powell, 2001).…”

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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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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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“…GNA is one of the most closely studied plant lectins, mainly because it was the first plant lectin shown to be active against Hemiptera and the protein is easy to purify (Shi et al, 1994;Hilder et al, 1995). It specifically binds to high-mannose glycans, in particular to terminal mannose residues.…”

Section: Gna: a Mannose-specific Lectin With Negative Effects On Sevementioning

confidence: 99%

Plant‐insect interactions: what can we learn from plant lectins?

Michiels

Damme

Smagghe

2010

Arch Insect Biochem Physiol

120

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Many plant lectins have high anti-insect potential. Although the effects of most lectins are only moderately influencing development or population growth of the insect, some lectins have strong insecticidal properties. In addition, some studies report a deterrent activity towards feeding and oviposition behavior. Transmission of plant lectins to the next trophic level has been investigated for several tritrophic interactions. Effects of lectins with different sugar specificities can vary substantially with the insect species under investigation and with the experimental setup. Lectin binding in the insect is an essential step in exerting a toxic effect. Attempts have been made to study the interactions of lectins in several insect tissues and to identify lectin-binding receptors. Ingested lectins generally bind to parts of the insect gut. Furthermore, some lectins such as the Galanthus nivalus agglutinin (GNA) cross the gut epithelium into the hemolymph and other tissues. Recently, several candidate lectinbinding receptors have been isolated from midgut extracts. To date little is known about the exact mechanism for insecticidal activity of plant lectins. However, insect glycobiology is an emerging research field and the recent Grant sponsor: Fund for Scientific Research-Flanders, Brussels; Grant number: 3G016306.Correspondence to: Guy Smagghe, Ghent University, Coupure Links 653, B-9000 Ghent, Belgium. E-mail: guy.smagghe@ugent.be Vol. 73, No. 4, 193-212 (2010 ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY,

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“…Controls containing no protein and containing no diet were set up for each trial. The diet solution was incorporated into feeding vessels based on those described by Hilder et al [4]. Petri dishes (90 mm diameter) were lined with water-soaked filter paper.…”

Section: Artificial Diet Bioassaysmentioning

confidence: 99%

“…Recent studies showed that some plant lectins were toxic to sapsucking insects in artificial diet assays [2,3], among which the lectin (GNA) from snowdrop (Galanthus nivalis), encoded by the gna gene, was the most toxic. Transgenic tobacco and rice expressing GNA showed significant insecticidal activity towards the peach potato aphids (Myzus persicae Sulzer) [4] and rice planthoppers including Nilaparvata lugens [5,6] and Laodelphax striatellus [7] respectively in bioassay and feeding tests.…”

Section: Introductionmentioning

confidence: 99%

Cloning and molecular characterization of a novel lectin gene from Pinellia ternata

et al. 2003

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The full-length cDNA of Pinellia ternata agglutinin (PTA) was cloned from inflorescences using RACE-PCR. Through comparative analysis of PTA gene (pta) and its deduced amino acid sequence with those of other Araceae species, pta was found to encode a precursor lectin with signal peptide and to have extensive homology with those of other Araceae species. PTA was a heterotetrameric mannose-binding lectin with three mannosebinding boxes like lectins from other Araceae and Amaryllidaceae species. Southern blot analysis of the genomic DNA revealed that pta belonged to a low-copy gene family. Northern blot analysis demonstrated that pta constitutively expressed in various plant tissues including root, leaf, stem and inflorescence. The pta cDNA sequence encoding for mature PTA protein was cloned into pET-32a plasmid and the resulting plasmid, pET32a-PTA containing Trx-PTA fusion protein, was investigated for the expression in E. coli BL21. SDS-PAGE gel analysis showed that the Trx-PTA fusion protein was successfully expressed in E. coli BL21 when induced by IPTG. Artificial diet assay revealed that PTA fusion protein had significant levels of resistance against peach potato aphids when incorporated into artificial diet at 0.1% (w/v). The cloning of the pta gene will enable us to further test its effect in depth on aphids by transferring the gene into crop plants.

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Expression of snowdrop lectin in transgenic tobacco plants results in added protection against aphids

Cited by 239 publications

References 21 publications

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

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

Plant‐insect interactions: what can we learn from plant lectins?

Cloning and molecular characterization of a novel lectin gene from Pinellia ternata

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