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Francisella tularensis subsp. holarctica releases differentially loaded outer membrane vesicles under various stress conditions

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F19%3A00537307" target="_blank" >RIV/60162694:G44__/19:00537307 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/19:00510313 RIV/44555601:13440/19:43894774

  • Result on the web

    <a href="https://www.frontiersin.org/articles/10.3389/fmicb.2019.02304/full" target="_blank" >https://www.frontiersin.org/articles/10.3389/fmicb.2019.02304/full</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3389/fmicb.2019.02304" target="_blank" >10.3389/fmicb.2019.02304</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Francisella tularensis subsp. holarctica releases differentially loaded outer membrane vesicles under various stress conditions

  • Original language description

    Francisella tularensis is a Gram-negative, facultative intracellular bacterium, causing a severe disease called tularemia. It secretes unusually shaped nanotubular outer membrane vesicles (OMV) loaded with a number of virulence factors and immunoreactive proteins. In the present study, the vesicles were purified from a clinical isolate of subsp. holarctica strain FSC200. We here provide a comprehensive proteomic characterization of OMV using a novel approach in which a comparison of OMV and membrane fraction is performed in order to find proteins selectively enriched in OMV vs. membrane. Only these proteins were further considered to be really involved in the OMV function and/or their exceptional structure. OMV were also isolated from bacteria cultured under various cultivation conditions simulating the diverse environments of F. tularensis life cycle. These included conditions mimicking the milieu inside the mammalian host during inflammation: oxidative stress, low pH, and high temperature (42°C); and in contrast, low temperature (25°C). We observed several-fold increase in vesiculation rate and significant protein cargo changes for high temperature and low pH. Further proteomic characterization of stress-derived OMV gave us an insight how the bacterium responds to the hostile environment of a mammalian host through the release of differentially loaded OMV. Among the proteins preferentially and selectively packed into OMV during stressful cultivations, the previously described virulence factors connected to the unique intracellular trafficking of Francisella were detected. Considerable changes were also observed in a number of proteins involved in the biosynthesis and metabolism of the bacterial envelope components like O-antigen, lipid A, phospholipids, and fatty acids. Data are available via ProteomeXchange with identifier PXD013074.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10606 - Microbiology

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>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2019

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Frontiers in Microbiology

  • ISSN

    1664-302X

  • e-ISSN

    1664-302X

  • Volume of the periodical

    10

  • Issue of the periodical within the volume

    Oct

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    16

  • Pages from-to

    2304

  • UT code for WoS article

    000491341100002

  • EID of the result in the Scopus database

    2-s2.0-85074161239