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Structure-functional study of PHL lectin from Photorhabdus asymbiotica

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00074015" target="_blank" >RIV/00216224:14740/14:00074015 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structure-functional study of PHL lectin from Photorhabdus asymbiotica

  • Original language description

    Lectins are a very important group of proteins and glycoproteins, which specifically recognize and reversibly bind glycoconjugates. Due to this interaction, lectins play a crucial role in many physiological and pathophysiological processes including immunological reactions or interactions between tissue?s cells. They also play a very important role in interactions between a pathogen and its host as they can mediate the first step of an expansion of infection. Our project is focused on study of a new lectin from the Photorhabdus asymbiotica bacterium. This bacterium is characterized as pathogen of both insects and humans. We have identified a new putative lectin (PHL) in the P. asymbiotica genome with the predicted structure similarity to the lectins from so-called AAL family, which are specific for fucosylated oligosaccharides.

  • Czech name

  • Czech description

Classification

  • Type

    O - Miscellaneous

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2014

  • Confidentiality

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