Binding of the insecticidal lectin Concanavalin A in pea aphid, Acyrthosiphon pisum (Harris) and induced effects on the structure of midgut epithelial cells

Sauvion, Nicolas; Nardon, C.; Febvay, Gérard; Gatehouse, A. M. R.; Rahbé, Yvan

doi:10.1016/j.jinsphys.2004.10.006

Cited by 86 publications

(58 citation statements)

References 55 publications

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“…Three modes of action of these dietary lectins have been identified: (1) binding of the lectins to the peritrophic matrix of the midgut and disrupting nutrient absorption (Harper et al, 1998); (2) binding to glycoproteins on epithelial cells of the midgut and disrupting tissue integrity (Powell et al, 1998;Sauvion et al, 2004); and (3) binding of lectins to carbohydrate moieties of the sensory receptors of the insect mouth parts, disrupting membrane integrity and interfering in the ability of the insects to detect food (Murdock and Shade, 2002). All three of these mechanisms result in decreased ability of the insects to ingest or absorb nutrients, leading to delayed development and premature death.…”

Section: Discussionmentioning

confidence: 99%

“…Although the mechanisms by which these insecticidal lectins act on insects are still not well understood, ultrastructural studies reveal that binding to insect gut structures and resistance to proteolytic degradation by insect digestive enzymes are the two main prerequisites for the lectins to have deleterious effects on insects (Sauvion et al, 2004). 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).…”

mentioning

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%

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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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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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

et al. 2008

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“…According to the direct toxic effect of lectins on insect biological parameters (Gatehouse et al 1984;Down et al 2003;Sauvion et al 2004) but also to the potential competitive effect of lectins towards viral particles in virus transmission by aphids, fungal lectins such as PeCL represent a very promising protein to control aphid pest damages in crops.…”

Section: Discussionmentioning

confidence: 99%

Purification of a new fungal mannose-specific lectin from Penicillium chrysogenum and its aphicidal properties

et al. 2011

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Lectin Mushroom Myzus persicaePenicillum chrysogenum Purification a b s t r a c t Several Ascomycetes fungi are commonly used in bio-industries and provide available industrial residues for lectin extraction to be valuable. A lectin from Penicillium chrysogenum, named PeCL, was purified from a fungal culture using gel-filtration chromatography column.PeCL was found to be a mannose-specific lectin by haemagglutination activity towards rabbit erythrocyte cells and was visualised on SDS-PAGE gel. Purified PeCL fraction was delivered via artificial diet to Myzus persicae aphid and was demonstrated to be aphicidal at 0.1 % with higher toxic efficiency than a known mannose-binding lectin Concanavalin A (ConA).A fast and efficient way to purify PeCL and a potential use in pest control is described.

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“…Later, the same group demonstrated that ConA also caused changes in feeding behavior (Sauvion et al, 2004a). In addition, using 14 C-tracing it was shown that significantly less lectin was excreted than was taken in by the insect (Sauvion et al, 2004b). ConA was found to bind primarily to the midgut and consequently to the whole digestive tract, and caused morphological changes in the epithelium cells as well as increased secretion and detachment of the apical membrane.…”

Section: Plant Lectins Principally Bind To Receptors In the Insect Gutmentioning

confidence: 98%

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

Michiels

Damme

Smagghe

2010

Arch Insect Biochem Physiol

118

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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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Binding of the insecticidal lectin Concanavalin A in pea aphid, Acyrthosiphon pisum (Harris) and induced effects on the structure of midgut epithelial cells

Cited by 86 publications

References 55 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

Purification of a new fungal mannose-specific lectin from Penicillium chrysogenum and its aphicidal properties

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

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