Plant Lectins

Damme, Els J.M. Van; Lannoo, Nausicaä; Peumans, Willy J.

doi:10.1016/s0065-2296(08)00403-5

Cited by 253 publications

(282 citation statements)

References 231 publications

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“…It seems likely, therefore, that type 2 RIPs were developed by a direct ancestor of modern seed plants. Until recently type 2 RIPs were believed to occur exclusively in flowering plants (Van Damme et al 2008). However, novel data leave no doubt that genuine homologs are also expressed in at least one species of the Gnetophyta.…”

Section: Other Proteins With Ricin-b Domainsmentioning

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: Other Proteins With Ricin-b Domainsmentioning

confidence: 99%

Evolution of Plant Ribosome-Inactivating Proteins

Peumans

Damme

2010

Toxic Plant Proteins

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“…Lectins are proteins that contain at least one noncatalytic domain that reversibly binds to specific glycans, which are present either in the free form or as parts of glycoproteins and glycolipids (Van Damme et al, 2008. Lectins have the unique ability to discriminate complex glycoconjugate structures without altering their molecular structure (Hirabayashi et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray diffraction studies of frutalin, an α-D-galactose-specific lectin fromArtocarpus incisaseeds

Monteiro-Moreira

Pereira²,

Neto

et al. 2015

Acta Cryst Sect F

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Frutalin is an -d-galactose-specific carbohydrate-binding glycoprotein with antitumour properties and is a powerful tool for tumour biomarker discovery. The crystallization and preliminary X-ray diffraction analysis of this lectin, which was isolated from Artocarpus incisa seeds, are reported here. Frutalin was purified and submitted to mass-spectrometric analysis. Diverse masses at approximately 16 kDa were observed in the deconvoluted spectra, which support the presence of isoforms. The best frutalin crystals were grown within a week in 0.1 M citric acid pH 3.5 which contained 25% PEG 3350 as a precipitant at 293 K, and diffracted to a maximum resolution of 1.81 Å . The monoclinic crystals belonged to space group I2, with unit-cell parameters a = 76.17, b = 74.56, c = 118.98 Å , = 96.56 . A molecular-replacement solution was obtained which indicated the presence of four monomers per asymmetric unit. Crystallographic refinement of the structure is in progress.

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“…Lectins/hemagglutinins, which are another important type of defense proteins, are found to be ubiquitously expressed at genome and transcriptome levels in plants 23 . This type of proteins is characterized by the unique property of initiating reversible and specific binding with carbohydrate structures.…”

Section: Resultsmentioning

confidence: 99%

Two legume defense proteins suppress the mobility of nasopharyngeal carcinoma cells

Dan

2016

Journal of Enzyme Inhibition and Medicinal Chemistry

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A 16-kDa trypsin inhibitor was isolated from an edible legume using various chromatographic procedures. The protein was unadsorbed on Affi-gel blue gel but adsorbed on DEAE-Sepharose and Mono Q following which media the protein was subsequently subjected to gel filtration on Superdex 75 and a final 21-fold purification was achieved. This trypsin inhibitor showed remarkable pH and thermal stability. Its inhibitory activity was impaired in the presence of 1 mM dithiothreitol. The anti-proliferative and anti-mobility activities of this trypsin inhibitor and a hemagglutinin isolated from the same legume were tested on nasopharyngeal carcinoma cells. These two defense proteins demonstrated discrepant anti-proliferative efficacies that the hemagglutinin could greatly suppress the proliferation of nasopharyngeal carcinoma cells, while the trypsin inhibitor revealed a minor effect. However, these two proteins could both attenuate the mobility of nasopharyngeal carcinoma cells. The present study revealed the potential of applying plant defense proteins in cancer treatment.

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Plant Lectins

Cited by 253 publications

References 231 publications

Evolution of Plant Ribosome-Inactivating Proteins

Evolution of Plant Ribosome-Inactivating Proteins

Crystallization and preliminary X-ray diffraction studies of frutalin, an α-D-galactose-specific lectin fromArtocarpus incisaseeds

Two legume defense proteins suppress the mobility of nasopharyngeal carcinoma cells

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