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Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00009310" target="_blank" >RIV/00216224:14310/03:00009310 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Moleular cloning and overexpression of bacterial lectins from human pathogen Pseudomonas aeruginosa involved in host-oligosaccharide recognition. Thermodynamical characterisation of lectin-monosaccharides interactions

  • Original language 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

  • Czech name

  • Czech description

Classification

  • Type

    D - Article in proceedings

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/ME%20675" target="_blank" >ME 675: Structural-functional study of bacterial viruses lectins.</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2003

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Article name in the collection

    European Congress of Young Chemists

  • ISBN

  • ISSN

  • e-ISSN

  • Number of pages

    1

  • Pages from-to

    70

  • Publisher name

    Chemical Scientific Set "Flogiston", Warsaw University of Technology

  • Place of publication

    Warsaw

  • Event location

    Zakopane

  • Event date

    Jan 1, 2003

  • Type of event by nationality

    EUR - Evropská akce

  • UT code for WoS article