Detailed Information on Publication Record
2007
Interesting behaviour of sugar-binding protein from phytopathogen Rasltonia solanacearum
ŠULÁK, Ondřej, Nikola KOSTLÁNOVÁ, Jan ADAM, Edward MITCHELL, Anne IMBERTY et. al.Basic information
Original name
Interesting behaviour of sugar-binding protein from phytopathogen Rasltonia solanacearum
Name in Czech
Zajímavý lektiny z fitopatogenu Ralstonia solanacearum
Authors
Edition
Brno, Konference Grantové Agentury České republiky, p. 28-77, 2007
Publisher
Masarykova univerzita
Other information
Language
English
Type of outcome
Stať ve sborníku
Field of Study
10600 1.6 Biological sciences
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
Organization unit
Faculty of Science
Keywords in English
Ralstonia solanacearum - lectin - crystallography
Změněno: 2/11/2007 17:22, Mgr. Ondřej Šulák, Ph.D.
V originále
Plant and animal pathogens use protein-carbohydrate interactions in their strategy for host recognition and invasion. The comprehension of the molecular mechanisms, which gives a pathogenic bacterium the ability to invade, colonize and reorient the physiopathology of its host, is a goal of primary importance and such studies may direct the conception of new strategies to fight against these pathogenic agents. Ralstonia solanacearum is a plant bacterial pathogen. It causes a wilt disease in several economically important agricultural crops, such as potatoes, tomatoes, peppers, eggplant and banana [1]. Cases of this disease are known as Southern wilt, bacterial wilt, and brown rot of potato. The disease is transmitted through soil, contaminated water, equipment, personnel, and by transplanting infected plants. It is not spread through the air, from plant to plant through the splashing of water. Lectins are sugar-binding proteins of non-immune nature that agglutinate cells or precipitate glycoconjugates. They recognize sugar moieties in cell walls or membranes and thereby change the physiology of the membrane to cause agglutination, mitosis, or other biochemical changes in the cell. Their specificity is usually defined by the monosaccharides or oligosaccharides that are the best at inhibiting the agglutination or precipitation induced by the lectin. Lectins are of interest because of their wide variety of properties and potential applications (pharmacology, immunology, cancer therapy, agriculture, etc.). As far as we know, the R. solanacearum bacterium has been producing three soluble lectins. RSL (MW 9900), which exhibits sugar specifity to L-fucose [2] and partial sequence homology to mushroom Aleuria aurantia lectin AAL [3], RS-IIL (MW 11601) lectin [4] resembles PA-IIL, from human pathogen Pseudomonas aeruginosa in structure and properties but differs in sugar specifity [5]. The last one is RS20L (MW 19903), which is described in the present study. This contribution structurally and functionally describes RS20L, which has no sequence similarity to any known amino acid sequence. Although resolution of crystal structure showed high structural similarity to animal galectins, it does not display sugar specifity to D-galactose. Further functional studies using gel permeation chromatography (GPC), surface plasmon resonance (SPR), isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC) allowed to define binding properties and thermodynamic parameters.
In Czech
Plant and animal pathogens use protein-carbohydrate interactions in their strategy for host recognition and invasion. The comprehension of the molecular mechanisms, which gives a pathogenic bacterium the ability to invade, colonize and reorient the physiopathology of its host, is a goal of primary importance and such studies may direct the conception of new strategies to fight against these pathogenic agents. Ralstonia solanacearum is a plant bacterial pathogen. It causes a wilt disease in several economically important agricultural crops, such as potatoes, tomatoes, peppers, eggplant and banana [1]. Cases of this disease are known as Southern wilt, bacterial wilt, and brown rot of potato. The disease is transmitted through soil, contaminated water, equipment, personnel, and by transplanting infected plants. It is not spread through the air, from plant to plant through the splashing of water. Lectins are sugar-binding proteins of non-immune nature that agglutinate cells or precipitate glycoconjugates. They recognize sugar moieties in cell walls or membranes and thereby change the physiology of the membrane to cause agglutination, mitosis, or other biochemical changes in the cell. Their specificity is usually defined by the monosaccharides or oligosaccharides that are the best at inhibiting the agglutination or precipitation induced by the lectin. Lectins are of interest because of their wide variety of properties and potential applications (pharmacology, immunology, cancer therapy, agriculture, etc.). As far as we know, the R. solanacearum bacterium has been producing three soluble lectins. RSL (MW 9900), which exhibits sugar specifity to L-fucose [2] and partial sequence homology to mushroom Aleuria aurantia lectin AAL [3], RS-IIL (MW 11601) lectin [4] resembles PA-IIL, from human pathogen Pseudomonas aeruginosa in structure and properties but differs in sugar specifity [5]. The last one is RS20L (MW 19903), which is described in the present study. This contribution structurally and functionally describes RS20L, which has no sequence similarity to any known amino acid sequence. Although resolution of crystal structure showed high structural similarity to animal galectins, it does not display sugar specifity to D-galactose. Further functional studies using gel permeation chromatography (GPC), surface plasmon resonance (SPR), isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC) allowed to define binding properties and thermodynamic parameters.
Links
| GD204/03/H016, research and development project |
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| MSM0021622413, plan (intention) |
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