Plant Lectins: A Composite of Several Distinct Families of Structurally and Evolutionary Related Proteins with Diverse Biological Roles

Damme, Els J.M. Van

doi:10.1016/s0735-2689(98)00365-7

Cited by 495 publications

(456 citation statements)

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“…According to the data published in previous research and review papers, the occurrence within the Viridiplantae of both the RIP and the ricin-B domain is confined to the Magnoliophyta (flowering plants) (Van Damme et al 1998;. To check whether these domains possibly occur in other taxa, a comprehensive analysis of the publicly accessible databases was made.…”

Section: General Overview Of the Taxonomic Distribution Of A And B Domentioning

confidence: 99%

Evolution of Plant Ribosome-Inactivating Proteins

Peumans

Damme

2010

Toxic Plant Proteins

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This contribution presents an updated analysis of the evolution of ribosome-inactivating proteins (RIPs) in plants. All evidence suggests that an ancestor of modern seed plants developed the RIP domain at least 300 million years ago. This ancestral RIP domain gave rise to a direct lineage of type 1 RIPs (i.e., primary type 1 RIPs) still present today in many monocots and at least one dicot. In a later stage, a plant succeeded in fusing the RIP domain to a duplicated ricin-B domain acquired from a bacterium. The resulting ancestral type 2 RIP gave rise to all modern type 2 RIPs and by domain deletion, to different lines of "secondary" type 1 RIPs and ricin-B type lectins. In the recent past, at least three other domain fusions took place in the Poaceae family, whereby type AC1 (type 3), type AC2, and type AD chimeric forms were generated.

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Section: General Overview Of the Taxonomic Distribution Of A And B Domentioning

confidence: 99%

Evolution of Plant Ribosome-Inactivating Proteins

Peumans

Damme

2010

Toxic Plant Proteins

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“…Some of these defense proteins are lectins (Chrispeels and Raikhel, 1991;Peumans and Van Damme, 1995;Czapala, 1997), which are widespread throughout the plant kingdom (Goldstein and Poretz, 1986). Plant lectins, also referred to as ''agglutinins,'' are a heterogenous group of carbohydratebinding proteins that are able to reversibly bind simple sugars and/or complex carbohydrates (for review, see Van Damme et al, 1998). However, over the past few years, novel sugar-binding domains have been identified (Kaku et al, 2006;Peumans et al, 2007;Van Damme et al, 2007a) that necessitated redefining the families of plant lectins.…”

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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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“…Observations of increasing numbers of lectins isolated from various vegetative storage organs, for example, bark, rhizomes and tubers, have also led to the suggestion that plant lectins have a dual function, to act as vegetative storage proteins (VSPs) and defense proteins. 2) Considering new criteria for the classification of plant lectins, in which seven families are proposed, 5) it might be appropriate to discuss functions with respect to individual lectin families or sub-families.…”

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confidence: 99%