A Novel Mannose-binding Tuber Lectin from Typhonium divaricatum (L.) Decne (family Araceae) with Antiviral Activity Against HSV-II and Anti-proliferative Effect on Human Cancer Cell Lines

Luo, Yi; Xu, Xiao-Chao; Liu, Jiwei; Li, Jian; Sun, Yisheng; Liu, Zhen; Liu, Jinzhi; Damme, Els J.M. Van; Balzarini, Jan; Bao, Ji

doi:10.5483/bmbrep.2007.40.3.358

Cited by 57 publications

(38 citation statements)

References 20 publications

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“…Amongst all the glycoproteins tested, mucin was the most effective hapten for RVL. Similar carbohydrate binding properties are reported for several monocot lectins like Colocasia esculenta lectin, Xanthosoma sagittifolium lectin, Arum maculatum lectin and Typhonium divaricatum lectin [10,13,22]. These lectins do not recognize mannose but strongly bind to asialofetuin and thyroglobulin, which are known to contain high mannose N-glycans and are referred to as Monocot mannose-binding lectins [13].…”

Section: Resultssupporting

confidence: 56%

“…Based on the potent inhibitory effect of some monocot mannose-binding lectins on human and animal retroviruses including HIV [16,17] and also on their ability to block the adhesion receptors of man-fimbriated E-coli in the small intestine [18], they can have potential applications in biomedical research. Recently some of the monocot mannose-binding lectins are reported to have antiproliferative and apoptosis inducing effects on different tumor cells [19][20][21][22][23]. Monocot mannose-binding lectins are being explored extensively for crop protection in plant biotechnology as many of them are reported to exhibit potent toxic effects on sucking pests and nematodes.…”

Section: Introductionmentioning

confidence: 99%

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Purification, characterization and molecular cloning of a monocot mannose-binding lectin from Remusatia vivipara with nematicidal activity

et al. 2010

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A mannose-binding lectin (RVL) was purified from the tubers of Remusatia vivipara, a monocot plant by single-step affinity chromatography on asialofetuin-Sepharose 4B. RVL agglutinated only rabbit erythrocytes and was inhibited by mucin, asialomucin, asialofetuin and thyroglobulin. Lectin activity was stable up to 80 degrees C and under wide range of pH (2.0-9.3). SDS-PAGE and gel filtration results showed the lectin is a homotetramer of Mr 49.5 kDa, but MALDI analysis showed two distinct peaks corresponding to subunit mass of 12 kDa and 12.7 kDa. Also the N-terminal sequencing gave two different sequences indicating presence of two polypeptide chains. Cloning of RVL gene indicated posttranslational cleavage of RVL precursor into two mature polypeptides of 116 and 117 amino-acid residues. Dynamic light scattering (DLS) and gel filtration studies together confirmed the homogeneity of the purified lectin and supported RVL as a dimer with Mr 49.5 kDa derived from single polypeptide precursor of 233 amino acids. Purified RVL exerts potent nematicidal activity on Meloidogyne incognita, a root knot nematode. Fluorescent confocal microscopic studies demonstrated the binding of RVL to specific regions of the alimentary-tract and exhibited a potent toxic effect on M. incognita. RVL-mucin complex failed to interact with the gut confirming the receptor mediated lectin interaction. Very high mortality (88%) rate was observed at lectin concentration as low as 30 microg/ml, suggesting its potential application in the development of nematode resistant transgenic-crops.

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Section: Resultssupporting

confidence: 56%

Section: Introductionmentioning

confidence: 99%

Purification, characterization and molecular cloning of a monocot mannose-binding lectin from Remusatia vivipara with nematicidal activity

et al. 2010

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“…The active fractions were pooled and dialyzed against 0.01 M buffer, then loaded onto a Sephadex 75 10/300 GL column pre-equilibrated with 0.01 M PBS ( pH 7.2), and then eluted with 0.1-0.5 M NaCl in the same buffer, at a flow rate of l ml/min. The active fractions were collected, dialyzed, and frozen for further study, according to previous procedures [18,19].…”

Section: Methodsmentioning

confidence: 99%

Isolation and characterization of a novel lectin with antifungal and antiproliferative activities from <italic>Sophora alopecuroides</italic> seeds

Li¹,

Yin²,

Liu³

et al. 2012

ABBS

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Sophora alopecuroides lectin (SAL), a novel lectin from the seeds of Sophora alopecuroides, was purified by ionexchange chromatography on diethylaminoethyl (DEAE)-and carboxymethyl (CM)-Sepharose columns, followed by gel filtration on a Sephadex 75 10/300 GL column. SAL was found to be a monomer of 39916.3 Da, as determined by tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis and high-performance liquid chromatography (HPLC). The N-terminal 10-amino acid sequence of SAL, KPWALSFSFG, resembles those of other legume lectins. SAL exhibits hemagglutinating activity against rabbit erythrocytes at 11.9 mg/ml. Its hemagglutinating activity is stable in the pH range 7-11 and in the temperature range 30 -908 8 8 8 8C, and is stimulated by Mn 21. The hemagglutinating activity of SAL is most potently inhibited by 50-mM D-galactose. SAL suppresses mycelial growth in Penicillium digitatum and Alternaria alternata; the IC 50 of the antifungal activity toward P. digitatum and A. alternata were found to be 3.125 and 3.338 mM, respectively. SAL suppresses the proliferation of human cervical cancer cells (HeLa) at an IC 50 of 6.25 mM (P < 0.05). But it has no inhibiting effect on bacteria. This is the first report of a lectin from seeds of S. alopecuroides.

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“…Lectins have received considerable attention for their potential therapeutic application in cancer (Sharon and Lis, 2002). Typhonium divaricatum lectin exhibits cytotoxicity against prostatic carcinoma Pro-01 and mastocarcinoma Bre-04 (Luo et al, 2007). Polygonatum cyrtonema lectin also induces apoptosis in cancer cells.…”

Section: Discussionmentioning

confidence: 99%

cDNA cloning, characterization, and pharmacologic evaluation of anticancer activity of a lectin gene in Pinellia integrifolia

2016

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ABSTRACT. Plant lectins are proteins that possess at least one non-catalytic domain, which could reversibly bind to specific monosaccharides or oligosaccharides. The important roles played by plant lectins in immune regulation, signaling pathways, and plant defense could be attributed to their specific binding activities with carbohydrates. In this study, a Pinellia integrifolia lectin gene, designated pia, was cloned using rapid amplification of cDNA ends. The open reading frame (ORF) of pia was constructed into the pET-28a vector, and a 33-kDa recombinant protein was induced in Escherichia coli BL21. The hemagglutination and anticancer properties of the purified recombinant protein were assayed in vitro. The results indicated that the full-length cDNA of pia was 1210 bp long, containing an 807-bp ORF encoding a 268-amino acid peptide. The putative P. integrifolia lectin protein (PIA) contained three mannose-binding sites. The agglutinating activity exhibited by PIA was inhibited by D-mannose. PIA was also shown to exert an anti-proliferative activity against nasopharyngeal carcinoma, human cervical carcinoma, and human breast cancer cell lines in vitro. These results could be applied to determine the function of PIA in the future.

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A Novel Mannose-binding Tuber Lectin from Typhonium divaricatum (L.) Decne (family Araceae) with Antiviral Activity Against HSV-II and Anti-proliferative Effect on Human Cancer Cell Lines

Cited by 57 publications

References 20 publications

Purification, characterization and molecular cloning of a monocot mannose-binding lectin from Remusatia vivipara with nematicidal activity

Purification, characterization and molecular cloning of a monocot mannose-binding lectin from Remusatia vivipara with nematicidal activity

Isolation and characterization of a novel lectin with antifungal and antiproliferative activities from <italic>Sophora alopecuroides</italic> seeds

cDNA cloning, characterization, and pharmacologic evaluation of anticancer activity of a lectin gene in Pinellia integrifolia

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A Novel Mannose-binding Tuber Lectin from Typhonium divaricatum (L.) Decne (family Araceae) with Antiviral Activity Against HSV-II and Anti-proliferative Effect on Human Cancer Cell Lines

Cited by 57 publications

References 20 publications

Purification, characterization and molecular cloning of a monocot mannose-binding lectin from Remusatia vivipara with nematicidal activity

Purification, characterization and molecular cloning of a monocot mannose-binding lectin from Remusatia vivipara with nematicidal activity

Isolation and characterization of a novel lectin with antifungal and antiproliferative activities from &lt;italic&gt;Sophora alopecuroides&lt;/italic&gt; seeds

cDNA cloning, characterization, and pharmacologic evaluation of anticancer activity of a lectin gene in Pinellia integrifolia

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Isolation and characterization of a novel lectin with antifungal and antiproliferative activities from <italic>Sophora alopecuroides</italic> seeds