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Sructure-function characterisation of a new lectin from Chromobacterium violaceum

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00013840" target="_blank" >RIV/00216224:14310/05:00013840 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Sructure-function characterisation of a new lectin from Chromobacterium violaceum

  • Original language description

    Carbohydrates are essential components of life that play crucial role in all organisms. They are very important agent in recognition and signalling ways. Lectin-carbohydrate interactions play a crucial role in many recognition events. Pseudomonas aeruginosa, an opportunistic pathogen responsible for numerous nosocomial infections in immunocopromised patients, produces a variety of carbohydrate-binding proteins that could be involved in host recognition and adhesion. One of them, PA-IIL, is a fucose binding lectin that is closely related to the virulence of the bacterium [1]. Searching in databases for proteins displaying sequence similarities to PA-IIL revealed new homologous proteins in other opportunistic pathogens like Chromobacterium violaceum. Human infection by Ch. violaceum is rare but when it occurs, it is associated with very high mortality rate [2]. In Ch. violaceum genome a hypothetical protein similar to PA-IIL and coded by the gene cv1741 was found. The gene was cloned and

  • Czech name

    Strukturně funkční charakterizace nového lektinu z bakterie Chromobacterium violaceum

  • Czech description

    Carbohydrates are essential components of life that play crucial role in all organisms. They are very important agent in recognition and signalling ways. Lectin-carbohydrate interactions play a crucial role in many recognition events. Pseudomonas aeruginosa, an opportunistic pathogen responsible for numerous nosocomial infections in immunocopromised patients, produces a variety of carbohydrate-binding proteins that could be involved in host recognition and adhesion. One of them, PA-IIL, is a fucose binding lectin that is closely related to the virulence of the bacterium [1]. Searching in databases for proteins displaying sequence similarities to PA-IIL revealed new homologous proteins in other opportunistic pathogens like Chromobacterium violaceum. Human infection by Ch. violaceum is rare but when it occurs, it is associated with very high mortality rate [2]. In Ch. violaceum genome a hypothetical protein similar to PA-IIL and coded by the gene cv1741 was found. The gene was cloned and

Classification

  • Type

    D - Article in proceedings

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2005

  • Confidentiality

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

Data specific for result type

  • Article name in the collection

    The FEBS Journal

  • ISBN

    1474-3833

  • ISSN

  • e-ISSN

  • Number of pages

    1

  • Pages from-to

    16

  • Publisher name

    FEBS Congres

  • Place of publication

    Budapest

  • Event location

    Budapest

  • Event date

    Jul 2, 2005

  • Type of event by nationality

    WRD - Celosvětová akce

  • UT code for WoS article