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Cooperation of both, the FKBP N-like and the DSBA-like, domains is necessary for the correct function of FTS 1067 protein involved in Francisella tularensis virulence and pathogenesis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F15%3A43875427" target="_blank" >RIV/60162694:G44__/15:43875427 - isvavai.cz</a>

  • Result on the web

    <a href="http://femspd.oxfordjournals.org/content/73/6/ftv030" target="_blank" >http://femspd.oxfordjournals.org/content/73/6/ftv030</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/femspd/ftv030" target="_blank" >10.1093/femspd/ftv030</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Cooperation of both, the FKBP N-like and the DSBA-like, domains is necessary for the correct function of FTS 1067 protein involved in Francisella tularensis virulence and pathogenesis

  • Original language description

    Francisella tularensis the etiological agent of tularaemia is one of the most infectious human pathogen known. Our knowledge about its key virulence factors has increased recently but it still remains a lot to explore. One of the described essential virulence factors is membrane lipoprotein FTS 1067 (nomenclature of F. tularensis subsp. holarctica strain FSC200) with homology to the protein family of disulphide oxidoreductases DsbA. Lipoprotein consists of two different domains: the C-terminal DsbA Com1-like domain (DSBA-like) and the N-terminal FKBP-type peptidyl-prolyl cis/trans isomerases (FKBP N-like). To uncover the biological role of these domains, we created bacterial strain with deletion of the DSBA-like domain. This defect in gene coding for lipoprotein FTS 1067 led to high in vivo attenuation associated with the ability to induce host protective immunity. Analyses performed with the truncated recombinant protein showed that the absence of DSBA-like domain revealed the loss of

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2015

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Pathogens and Disease

  • ISSN

    2049-632X

  • e-ISSN

  • Volume of the periodical

    73

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    12

  • Pages from-to

    "Article Number: UNSP ftv030"

  • UT code for WoS article

    000362574300002

  • EID of the result in the Scopus database