Action of a nematode-trapping fungus shows lectin-mediated host–microorganism interaction

Nordbring‐Hertz, Birgit; Mattìasson, Bo

doi:10.1038/281477a0

Cited by 141 publications

(58 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Fungi, either mushrooms or filamentous fungi, often depend on host association (symbiosis or parasitism) and appear to use lectins for host recognition and/or adhesion. One of the first examples of a lectin-mediated interaction between a fungus and its host was discovered in the nematode-trapping fungus Arthrobotrys oligospora (2). In higher fungi, lectins are involved in molecular recognition during the early stage of mycorrhization.…”

mentioning

confidence: 99%

“…Harker sections of the anomalous difference Patterson map showed two peaks corresponding to one mercury per monomer in the asymmetric unit. Initial mercury site coordinates, phasing, and solvent flattening were carried out with autoSHARP (25), 2 which located the two mercury sites. autoSHARP was also directed to search for noncrystallographic symmetry, and the resulting matrix was further refined, together with averaging and phase extension, using DM (27) to give an electron density map of excellent quality.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Crystal Structure of Fungal Lectin

Wimmerová

Mitchell

Sanchez

et al. 2003

Journal of Biological Chemistry

169

102

View full text Add to dashboard Cite

Aleuria aurantia lectin is a fungal protein composed of two identical 312-amino acid subunits that specifically recognizes fucosylated glycans. The crystal structure of the lectin complexed with fucose reveals that each monomer consists of a six-bladed ␤-propeller fold and of a small antiparallel two-stranded ␤-sheet that plays a role in dimerization. Five fucose residues were located in binding pockets between the adjacent propeller blades. Due to repeats in the amino acid sequence, there are strong similarities between the sites. Oxygen atoms O-3, O-4, and O-5 of fucose are involved in hydrogen bonds with side chains of amino acids conserved in all repeats, whereas O-1 and O-2 interact with a large number of water molecules. The nonpolar face of each fucose residue is stacked against the aromatic ring of a Trp or Tyr amino acid, and the methyl group is located in a highly hydrophobic pocket. Depending on the precise binding site geometry, the ␣-or ␤-anomer of the fucose ligand is observed bound in the crystal. Surface plasmon resonance experiments conducted on a series of oligosaccharides confirm the broad specificity of the lectin, with a slight preference for ␣Fuc1-2Gal disaccharide. This multivalent carbohydrate recognition fold is a new prototype of lectins that is proposed to be involved in the host recognition strategy of several pathogenic organisms including not only the fungi Aspergillus but also the phytopathogenic bacterium Ralstonia solanacearum.

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

Crystal Structure of Fungal Lectin

Wimmerová

Mitchell

Sanchez

et al. 2003

Journal of Biological Chemistry

169

102

View full text Add to dashboard Cite

show abstract

“…Así mismo, se detectó que la formación de redes tridimensionales es la principal estructura de atrapamiento de estos dos hongos, resultados coincidentes con registros internacionales (12,22,(26)(27)(28)(29).…”

Section: Discussionunclassified

Capacidad predadora in vitro de hongos nematófagos nativos de Cundinamarca sobre nematodos gastrointestinales de bovinos

Lara¹,

Burbano²,

Cárdenas³

et al. 2015

Rev. Med. Vet.

View full text Add to dashboard Cite

La dependencia y el uso indiscriminado de antihelmínticos químicos como único método de control de los nematodos gastrointestinales (NGI) de bovinos ocasiona problemas en el medio ambiente, la salud pública y la productividad de la ganadería bovina. Es necesario desarrollar estrategias no químicas de control. Los hongos nematófagos pueden ser una alternativa viable y promisoria para el control de estos endoparásitos. El objetivo de este estudio fue aislar, identificar y evaluar in vitro el potencial nematófago de hongos de Cundinamarca sobre larvas L3 de NGI de bovinos. Se sembraron 60 muestras de suelo de fincas ganaderas en cajas de Petri con medio agar-agua para el atrapamiento de los hongos, y se identificaron mediante claves morfométricas tres cepas del hongo Arthrobotrys oligospora (L1, XVIII y XXI) y una de Arthrobotrys musiformis (XXIV). Se utilizaron 1 × 106 conidios o clamidosporas de cada hongo, los cuales se enfrentaron a 100 larvas de nematodos. El aislamiento XXIV (A. musiformis) demostró mayor capacidad predadora (96,8 %) que los aislamientos (A. oligospora) XVIII, L1 y XXI (69, 68, 71,1 y 87,62 %, respectivamente). No hubo diferencias estadísticamente significativas (p > 0,05) entre las cepas de mayor capacidad predadora. Este es el primer registro de identificación y evaluación in vitro de la capacidad predadora de los hongos A. oligospora y A. musiformis nativos de Cundinamarca. Los resultados sugieren que estos hongos podrían emplearse como agentes biocontroladores de nematodos de bovinos.

show abstract

“…The A. oligospora lectin was identified in the fungus as responsible for the capture of the host that takes place through its interaction with a receptor bearing the specific carbohydrate present on the nematode surface (50). This mechanism of adhesion to host surfaces is believed to be present in many other both parasitic and symbiotic fungi.…”

Section: Resultsmentioning

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

View full text Add to dashboard Cite

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.

show abstract

Action of a nematode-trapping fungus shows lectin-mediated host–microorganism interaction

Cited by 141 publications

References 16 publications

Crystal Structure of Fungal Lectin

Crystal Structure of Fungal Lectin

Capacidad predadora in vitro de hongos nematófagos nativos de Cundinamarca sobre nematodos gastrointestinales de bovinos

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

Contact Info

Product

Resources

About