Structural requirements of carbohydrates to bind Agaricus bisporus lectin

Irazoqui, Fernando J.; Vides, Miguel A.; Nores, Gustavo A.

doi:10.1093/glycob/9.1.59

Cited by 32 publications

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“…There are four well known dietary TFbinding lectins: the mushroom lectin (ABL) from the common edible mushroom Agaricus bisporus, jacalin (JAC) from the seeds of jackfruit Artocarpus integrifolia eaten in India and parts of the Far East, the peanut lectin (PNA) from peanut Arachis hypogaea, and amaranth lectin (ACA) from Amaranthus caudatus, which used to be an important food source in South America and is becoming re-established as a food. All four lectins lack cytotoxicity, can be eaten raw with apparent impunity and recognise the TF antigen, but Chen et al, 1995;Irazoqui et al, 1999). The four lectins have also been used in histochemistry for identi®cation of the TF antigen in tissue (Boland et al, 1991;Cao et al, 1996;Kabir, 1998;Saussez et al, 1998).…”

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Opposite effects on human colon cancer cell proliferation of two dietary Thomsen-Friedenreich antigen-binding lectins

Milton

Fernig

et al. 2001

J. Cell. Physiol.

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Increased cell surface expression of the Thomsen-Friedenreich antigen (TF antigen, Galbeta1-3GalNAcalpha-) is a common feature in malignant and pre-malignant epithelia. Our previous studies have shown that dietary TF-binding lectins from peanut (Arachis hypogea) and edible mushroom (Agaricus bisporus) produce marked but different effects on human intestinal epithelial cell proliferation. This study investigates the proliferative effects of the other two known dietary TF-binding lectins: jacalin (Artocarpus integrifolia, JAC) and amaranth lectin (Amaranthus caudatus, ACA). JAC produced dose-dependent and non-cytotoxic inhibition of proliferation in HT29 human colon cancer cells with maximal effects of 46 +/- 4% at 20 microg/ml, whereas ACA produced dose-dependent stimulation of proliferation with maximal effects of 22 +/- 3% at 20 microg/ml when assessed both by incorporation of [3H]thymidine into DNA and by cell counting. The lectin-mediated effects were inhibitable by the presence of appropriate Galbeta1-3GalNAc-expressing glycoproteins but differences existed between JAC and ACA in their patterns of inhibition by such substances. Ligand binding equilibrium studies using iodinated lectins revealed different Kd of the two lectins for HT29 cell surface glycoproteins. Lectin blots of cell membrane extracts showed different binding patterns in all the four TF-binding lectins. These results provide further evidence that dietary TF-binding lectins can have marked effects on the proliferation of human malignant gastro-intestinal epithelial cells and hence may play a role in intestinal cancer development, and also show that the biological effects of dietary lectins cannot be predicted solely from their carbohydrate binding properties.

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confidence: 99%

Opposite effects on human colon cancer cell proliferation of two dietary Thomsen-Friedenreich antigen-binding lectins

Milton

Fernig

et al. 2001

J. Cell. Physiol.

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“…Fungal lectins have recently been reviewed (7)(8)(9). However, apart from the lectin from A. bisporus, which binds to Gal␤1,3GalNAc␣-Ser/Thr (T-disaccharide) (10), the detailed carbohydrate specificities of these fungal lectins have not been investigated in depth.…”

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confidence: 99%

Purification and Characterization of a Neu5Acα2–6Galβ1–4Glc/GlcNAc-specific Lectin from the Fruiting Body of the Polypore Mushroom Polyporus squamosus

Winter

Goldstein

2000

Journal of Biological Chemistry

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A lectin has been purified from the carpophores of the mushroom Polyporus squamosus by a combination of affinity chromatography on ␤-D-galactosyl-Synsorb and ion-exchange chromatography on DEAE-Sephacel. Gel filtration chromatography, SDS-polyacrylamide gel electrophoresis, and N-terminal amino acid sequencing indicated that the native lectin, designated P. squamosus agglutinin, is composed of two identical 28-kDa subunits associated by noncovalent bonds. P. squamosus agglutinin agglutinated human A, B, and O and rabbit red blood cells but precipitated only with human ␣ 2 -macroglobulin, of many glycoproteins and polysaccharides tested. The detailed carbohydrate binding properties of the purified lectin were elucidated using three different approaches, i.e. precipitation inhibition assay (in solution binding assay), fluorescence quenching studies, and glycolipid binding by lectin staining on high-performance thin layer chromatography (solid-phase binding assay). Based on the results obtained by these assays, we conclude that although the P. squamosus lectin binds ␤-D-galactosides, it has an extended carbohydratecombining site that exhibits highest specificity and affinity toward nonreducing terminal Neu5Ac␣2,6Gal␤1,4Glc/GlcNAc (6-sialylated type II chain) of N-glycans (2000-fold stronger than toward galactose). The strict specificity of the lectin for ␣2,6-linked sialic acid renders this lectin a valuable tool for glycobiological studies in biomedical and cancer research.

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“…Four other well characterized lectins known to recognize the TF structures are ACA, ABL, PNA and Jacalin [13][14][15][16][17]. In comparison with these TF binding lectins, SRL shows differences in its carbohydrate binding properties and the observed differences are summarized in Table 7.…”

Section: Discussionmentioning

confidence: 99%

“…Although SRL recognizes TF disaccharide (Galβ1-3Gal-NAc) and its substituted forms, it does not recognize disaccharides like Lacto-N-biose (G# 133; Galβ1-3GlcNAc) and LacNAc (G# 152; Galβ1-4GlcNAc), which are conformationally related disaccharides. This is in contrast to the binding of ABL [14], Jacalin [16] and ACA [13]. On the other hand PNA recognizes both the disaccharides; Lacto-Nbiose and LacNAc [15].…”

Section: Discussionmentioning

confidence: 99%

Exquisite binding specificity of Sclerotium rolfsii lectin toward TF-related O-linked mucin-type glycans

Chachadi

Rhodes

et al. 2011

Glycoconj J

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Sclerotium rolfsii lectin (SRL), a secretory protein from the soil borne phytopathogenic fungus Sclerotium rolfsii, has shown in our previous studies to bind strongly to the oncofetal Thomson-Friedenreich carbohydrate (Galβ1-3GalNAc-ser/thr, T or TF) antigen. TF antigen is widely expressed in many types of human cancers and the strong binding of SRL toward such a cancer-associated carbohydrate structure led us to characterize the carbohydrate binding specificity of SRL. Glycan array analysis, which included 285 glycans, shows exclusive binding of SRL to the O-linked mucin type but not N-linked glycans and amongst the mucin type O-glycans, lectin recognizes only mucin core 1, core 2 and weakly core 8 but not to other mucin core structures. It binds with high specificity to "α-anomers" but not the "β-anomers" of the TF structure. The axial C4-OH group of GalNAc and C2-OH group of Gal is both essential for SRL interaction with TF disaccharide, and substitution on C3 of galactose by sulfate or sialic acid or N-acetylglucosamine, significantly enhances the avidity of the lectin. SRL differs in its binding to TF structures compared to other known TF-binding lectins such as the Arachis hypogea (peanut) agglutinin, Agaricus bisporus (mushroom) lectin, Jackfruit, Artocarpus integrifolia (jacalin) and Amaranthus caudatus (Amaranthin) lectin. Thus, SRL has unique carbohydrate-binding specificity toward TF-related O-linked carbohydrate structures. Such a binding specificity will make this lectin a very useful tool in future structural as well as functional analysis of the cellular glycans in cancer studies.

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Structural requirements of carbohydrates to bind Agaricus bisporus lectin

Cited by 32 publications

References 32 publications

Opposite effects on human colon cancer cell proliferation of two dietary Thomsen-Friedenreich antigen-binding lectins

Opposite effects on human colon cancer cell proliferation of two dietary Thomsen-Friedenreich antigen-binding lectins

Purification and Characterization of a Neu5Acα2–6Galβ1–4Glc/GlcNAc-specific Lectin from the Fruiting Body of the Polypore Mushroom Polyporus squamosus

Exquisite binding specificity of Sclerotium rolfsii lectin toward TF-related O-linked mucin-type glycans

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