Isolation and Characterization of a cDNA Clone Encoding a Lectin Gene from Agaricus bisporus

Crenshaw, R W; Harper, S N; Moyer, Mary B.; Privalle, Laura

doi:10.1104/pp.107.4.1465

Cited by 40 publications

(23 citation statements)

References 5 publications

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“…The binding specificity to GalP3GalNAccx-SerlThr is similar to that identified for a lectin (designated ABL) isolated from the mushroom Agariccts bisporus [6, 71. The obtained data show that the primary structure of AOL has a high sequence similarity to the deduced amino acid sequence of a recently published cDNA clone of ABL [8], but not to any other fungal, plant or animal lectins. These findings indicate that AOL and ABL are members of a novel family of saline-soluble lectins present in fungi sharing similar primary structures and binding properties.…”

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confidence: 61%

“…The EMBL and Swiss-Prot data banks were searched for sequences similar to the nucleotide and deduced amino acid sequence of the AOL gene. A high sequence similarity (46.3 % identity, 61.8 % similarity) was observed between the deduced amino acid sequence of the AOL gene and that deduced from a a recently published cDNA clone encoding a soluble lectin (ABL) isolated from the basidiomycete Agaricus bisporus [8] (Fig. 3).…”

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confidence: 73%

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Molecular Characterization of a Saline‐Soluble Lectin from a Parasitic Fungus

Rosén

Kata

Persson

et al. 1996

European Journal of Biochemistry

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It has been proposed that the interactions between several parasitic and pathogenic fungi and their hosts are mediated by soluble lectins present in the fungus. We have cloned and analyzed a gene encoding such a lectiii (AOL) from the nematophagous fungus Arthr.obotr.y,v oligospora (deuteromycete). The deduced primary structure of the AOL gene displayed an extensive similarity (identity 46.3 %) to that of a gene encoding a lectin (ABL) recently isolated from the mushroom Agaricus bisporus (basidiomycete), but not to any other fungal, microbial, plant or animal lectins. The similarities between AOL and ABL were further demonstrated by the observation that an antibody specific for AOL cross-reacted with ABL. Together with data showing that AOL has a binding specificity that is similar to that of ABL [Rostn, S., Bergstrom, J., Karlsson, K.-A. & Tunlid, A. (1996) Eur. I. Biochem. 238, 830-8371, these results indicate that AOL and ABL are members of a novel family of saline-soluble lectins present in fungi. Southern blots indicated that there is only one AOL gene in the genome encoding a subunit (monomer) of the lectin. The primary structure of AOL did not show the presence of a typical N-terminal signal sequence. Comparison of the deduced primary structure with the molecular mass of AOL as determined by electrospray mass spectrometry (16 153 Da), indicated that AOL has an acetylated N-terminal but no other posttranslational modifications, and that a minor isoform is formed by deamidation. Circular dichroism (CD) spectroscopy suggested that the secondary structure of AOL contains 34% P-sheets, 21 % u-helix, and 45% turns and coils.Keywords; fungal lectin ; primary structure ; secondary structure ; electrospray mass spectrometry.Lectins are a diverse group of carbohydrate-binding proteins commonly present in aflimals, plants, and microorganisms. The biological function of many lectins is not clear, but there is increasing evidence that lectins can act as mediators of cellular and molecular recognition in a wide range of biological systems [l]. One of the first examples indicating a lectin-mediated interaction in a fungal-host system was in the nematode-trapping fungus Arthrobotrys oligospora [2]. This fungus captures nematodes by using adhesive polymers present on special hyphae called traps. Results from inhibition experiments using various soluble carbohydrates indicated that the adhesion was initiated by a GalNAc-specific lectin in the fungus binding to a carbohydrate receptor present on the nematode surface. Later, similar experiments have indicated that lectins could be involved in the adhesion to host surfaces in a number of both parasitic and sym- [3]. Even though lectins have been isolated from several of these fungi, details of their structure, binding properties, and localization, which are important for understanding their function at a molecular level. are not well known.In this paper, we have cloned and analyzed a gene encoding a lectin from a parasitic fungus. The lectin (designated AOL) was previously...

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confidence: 61%

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confidence: 73%

Molecular Characterization of a Saline‐Soluble Lectin from a Parasitic Fungus

Rosén

Kata

Persson

et al. 1996

European Journal of Biochemistry

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“…Amino Acid Sequence-The 2.5 Å high quality electron density map of the orthorhombic crystals was very straightforward to interpret from Thr 2 to Gly 133 in terms of the translated sequence of the cDNA coding for the protein (12). However, when this point in the chain trace was reached, it became evident that there was no longer correspondence between electron density and amino acid sequence and also that the chain appeared to be shorter than predicted by the published sequence.…”

Section: Resultsmentioning

confidence: 98%

“…The initial model of the apoprotein was built in the high quality map at 2.5 Å resolution using the program O (23). Model building proceeded without difficulty from Thr 2 to Gly 133 following the sequence from nucleic acid available at the ExPASy server (12). At this point, two facts became evident: the first was that the electron density did not match the published sequence, and the second was that there was no electron density in the map beyond amino acid 143 (the published sequence is 154 amino acid long).…”

Section: Protein Purification and Crystallization-abl Was Purified Frommentioning

confidence: 99%

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The Antineoplastic Lectin of the Common Edible Mushroom (Agaricus bisporus) Has Two Binding Sites, Each Specific for a Different Configuration at a Single Epimeric Hydroxyl

Carrizo

Capaldi

Perduca

et al. 2005

Journal of Biological Chemistry

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The lectin from the common mushroom Agaricus bisporus, the most popular edible species in Western countries, has potent antiproliferative effects on human epithelial cancer cells, without any apparent cytotoxicity. This property confers to it an important therapeutic potential as an antineoplastic agent. The three-dimensional structure of the lectin was determined by x-ray diffraction. The protein is a tetramer with 222 symmetry, and each monomer presents a novel fold with two ␤ sheets connected by a helix-loop-helix motif. Selectivity was studied by examining the binding of four monosaccharides and seven disaccharides in two different crystal forms. The T-antigen disaccharide, Gal␤1-3GalNAc, mediator of the antiproliferative effects of the protein, binds at a shallow depression on the surface of the molecule. The binding of N-acetylgalactosamine overlaps with that moiety of the T antigen, but surprisingly, Nacetylglucosamine, which differs from N-acetylgalactosamine only in the configuration of epimeric hydroxyl 4, binds at a totally different site on the opposite side of the helix-loop-helix motif. The lectin thus has two distinct binding sites per monomer that recognize the different configuration of a single epimeric hydroxyl. The structure of the protein and its two carbohydrate-binding sites are described in detail in this study.

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Isolation and characterization of a novel thermostable lectin from the wild edible mushroom Agaricus arvensis

Zhao

et al. 2011

J. Basic Microbiol.

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A thermostable novel lectin with a molecular weight of 30.4 kDa was isolated from dried fruiting bodies of Agaricus arvensis. It was a dimer made up of two 15.2 kDa subunits. The lectin was unadsorbed on DEAE-cellulose in 10 mM phosphate buffer (pH 7.5), subsequently adsorbed on CM-cellulose in 10 mM NaAc buffer (pH 4.6) and then on SP-Sepharose in 10 mM NaAc buffer (pH 4.6), and finally purified by fast protein liquid chromatography-gel filtration on Superdex 75. The hemagglutinating activity of the lectin was stable at temperatures up to 90 °C. The activity was preserved in concentrations of NaOH solution up to 50 mM, but was sensitive to HCl and declined to 12.5% in 12.5 mM HCl. The activity was unaffected by Ca(2+), Mn(2+), Zn(2+) and Mg(2+) ions, but was activated by Al(3+) and Fe(3+) ions. Among the carbohydrates tested, only inulin could inhibit the hemagglutinating activity of the lectin. It did not exhibit anti-HIV reverse transcriptase activity. Proliferation of HepG2 and MCF7 tumor cells was inhibited by the lectin with an IC(50) of 1.64 and 0.82 μM, respectively. The lectin was devoid of antifungal activity. The lectin has a remarkable thermostablity and a unique N-terminal amino acid sequence, TYAVLNFVYG. The present report is the first report on a lectin from wild mushroom Agaricus arvensis.

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Isolation and Characterization of a cDNA Clone Encoding a Lectin Gene from Agaricus bisporus

Cited by 40 publications

References 5 publications

Molecular Characterization of a Saline‐Soluble Lectin from a Parasitic Fungus

Molecular Characterization of a Saline‐Soluble Lectin from a Parasitic Fungus

The Antineoplastic Lectin of the Common Edible Mushroom (Agaricus bisporus) Has Two Binding Sites, Each Specific for a Different Configuration at a Single Epimeric Hydroxyl

Isolation and characterization of a novel thermostable lectin from the wild edible mushroom Agaricus arvensis

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