| Attributes | Values |
|---|
| rdf:type
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| Description
| - Human pathogenic bacteria Pseudomonas aeruginosa colonize patients with a number of chronic lung diseases and is a major cause of morbidity and mortality in cystic fibrosis patients. Specific oligosaccharide-mediated recognition and adhesion are key points in the initiating steps of the P. aeruginosa infection. The bacterium produces two sugar-recognising proteins PA-IL (LecA) and PA-IIL (LecB), galactose- and fucose-binding lectins respectively, that can play a crucial role in adhesion and specific recognition of a host by the pathogen and contribute to its virulence. Recently, the crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A[1]. P. aeruginosa expresses these lectins under stressed conditions that limit their in vitro production for further structure-functional characterisation. Therefore, both lecA and lecB genes were cloned into pET25 vector, expressed in E.coli BL21(DE3) cells as host organism and purified by affinity chromatography on Sepharose 4B and Mannose-agarose
- Human pathogenic bacteria Pseudomonas aeruginosa colonize patients with a number of chronic lung diseases and is a major cause of morbidity and mortality in cystic fibrosis patients. Specific oligosaccharide-mediated recognition and adhesion are key points in the initiating steps of the P. aeruginosa infection. The bacterium produces two sugar-recognising proteins PA-IL (LecA) and PA-IIL (LecB), galactose- and fucose-binding lectins respectively, that can play a crucial role in adhesion and specific recognition of a host by the pathogen and contribute to its virulence. Recently, the crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A[1]. P. aeruginosa expresses these lectins under stressed conditions that limit their in vitro production for further structure-functional characterisation. Therefore, both lecA and lecB genes were cloned into pET25 vector, expressed in E.coli BL21(DE3) cells as host organism and purified by affinity chromatography on Sepharose 4B and Mannose-agarose (en)
- Human pathogenic bacteria Pseudomonas aeruginosa colonize patients with a number of chronic lung diseases and is a major cause of morbidity and mortality in cystic fibrosis patients. Specific oligosaccharide-mediated recognition and adhesion are key points in the initiating steps of the P. aeruginosa infection. The bacterium produces two sugar-recognising proteins PA-IL (LecA) and PA-IIL (LecB), galactose- and fucose-binding lectins respectively, that can play a crucial role in adhesion and specific recognition of a host by the pathogen and contribute to its virulence. Recently, the crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A[1]. P. aeruginosa expresses these lectins under stressed conditions that limit their in vitro production for further structure-functional characterisation. Therefore, both lecA and lecB genes were cloned into pET25 vector, expressed in E.coli BL21(DE3) cells as host organism and purified by affinity chromatography on Sepharose 4B and Mannose-agarose (cs)
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| Title
| - Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions
- Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions (en)
- Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions (cs)
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| skos:prefLabel
| - Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions
- Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions (en)
- Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions (cs)
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| skos:notation
| - RIV/00216224:14310/03:00009310!RIV08-MSM-14310___
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| http://linked.open.../vavai/riv/strany
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
| - P(ME 675), Z(MSM 143100005)
|
| http://linked.open...vai/riv/dodaniDat
| |
| http://linked.open...aciTvurceVysledku
| |
| http://linked.open.../riv/druhVysledku
| |
| http://linked.open...iv/duvernostUdaju
| |
| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14310/03:00009310
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| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - pseudomonas aeruginosa; lectin; cloning (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...v/mistoKonaniAkce
| |
| http://linked.open...i/riv/mistoVydani
| |
| http://linked.open...i/riv/nazevZdroje
| - European Congress of Young Chemists
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| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...iv/tvurceVysledku
| - Imberty, Anne
- Pokorná, Martina
- Wimmerová, Michaela
- Gilboa-Garber, Nechama
- Sabin, Charles
|
| http://linked.open...vavai/riv/typAkce
| |
| http://linked.open.../riv/zahajeniAkce
| |
| http://linked.open...n/vavai/riv/zamer
| |
| number of pages
| |
| http://purl.org/ne...btex#hasPublisher
| - Chemical Scientific Set %22Flogiston%22, Warsaw University of Technology
|
| http://localhost/t...ganizacniJednotka
| |
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