A New Lectin Family with Structure Similarity to Actinoporins Revealed by the Crystal Structure of Xerocomus chrysenteron Lectin XCL

Birck, Catherine; Damian, Luminita; Marty-Detraves, Claire; Lougarre, Andrée; Schulze-Briese, Clemens; Koehl, Patrice; Fournier, Didier; Paquereau, Laurent; Samama, Jean‐Pierre

doi:10.1016/j.jmb.2004.10.007

Cited by 63 publications

(55 citation statements)

References 45 publications

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“…1). SRL was shown to be a dimer but can, from a structural point of view, form similar tetramers as other representatives (Birck et al 2004;Bovi et al 2011;Carrizo et al 2005;Leonidas et al 2007).…”

Section: Actinoporin-type Lectinsmentioning

confidence: 99%

“…Homodimer 4 Gal na Entomotoxic (Hamshou et al 2013;Hamshou et al 2010b;Hamshou et al 2012;Skamnaki et al 2013) Bleuler-Martinez et al 2011;Fujihashi et al 2003;Fukumori et al 1990;Kochibe and Furukawa 1980;Olausson et al 2010;Olausson et al 2008;Tateno et al 2009;Wimmerova et al 2003) GlcNAc-β1,4-X na nd (Cioci et al 2006;Ueda et al 1999a;Ueda et al 2002;Ueda et al 1999b;Ueda et al 2003) Entomotoxic (Birck et al 2004;Bleuler-Martinez et al 2011;Damian et al 2005;Francis et al 2003;Jaber et al 2008;Jaber et al 2007;…”

Section: β-Trefoilmentioning

confidence: 99%

“…Members of this protein family show structural homology to actinoporins, a family of pore-forming proteins (cytolysins) originally isolated from sea anemones (Birck et al 2004;Kristan et al 2009). It was suggested that the archetypal actinoporin fold is used for specific binding to various molecules at the plasma membrane surface (Kristan et al 2009).…”

Section: Actinoporin-type Lectinsmentioning

confidence: 99%

“…It was suggested that the archetypal actinoporin fold is used for specific binding to various molecules at the plasma membrane surface (Kristan et al 2009). Characterized representatives of the actinoporin-type mushroom lectin family include XCL, ABL (ABA), SRL, and BEL from the basidiomycetes Xerocomus (Boletus) chrysenteron, Agaricus bisporus, Sclerotium (Athelia) rolfsii, and B. edulis (Birck et al 2004;Bovi et al 2011;Carrizo et al 2005;Leonidas et al 2007) and AOL 2 and TAP1 from the ascomycetes Arthrobotrys oligospora and Sordaria macrospora (Nowrousian and Cebula 2005;Rosen et al 1996b). These representatives of basidiomycetes share 53 to 82 % sequence identity (67 to 89 % similarity), while AOL 2 is approximately 45 % identical (62 % similar) to them and TAP1 only 34 % identical (50 % similar).…”

Section: Actinoporin-type Lectinsmentioning

confidence: 99%

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Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

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Section: Actinoporin-type Lectinsmentioning

confidence: 99%

Section: β-Trefoilmentioning

confidence: 99%

Section: Actinoporin-type Lectinsmentioning

confidence: 99%

Section: Actinoporin-type Lectinsmentioning

confidence: 99%

See 2 more Smart Citations

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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“…Note Added in Proof-A study with the determination of the threedimensional structure of the X. chrysenteron lectin has been published recently (61).…”

mentioning

confidence: 99%

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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Structural Features of Lectins and Their Binding Sites

Loris

2009

Bioinformatics for Glycobiology and Glycomics

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A New Lectin Family with Structure Similarity to Actinoporins Revealed by the Crystal Structure of Xerocomus chrysenteron Lectin XCL

Cited by 63 publications

References 45 publications

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

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

Structural Features of Lectins and Their Binding Sites

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