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Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00482215" target="_blank" >RIV/61388971:_____/17:00482215 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/17:10366606

  • Result on the web

    <a href="http://dx.doi.org/10.3390/toxins9100300" target="_blank" >http://dx.doi.org/10.3390/toxins9100300</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/toxins9100300" target="_blank" >10.3390/toxins9100300</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes

  • Original language description

    Bordetellae, pathogenic to mammals, produce an immunomodulatory adenylate cyclase toxin-hemolysin (CyaA, ACT or AC-Hly) that enables them to overcome the innate immune defense of the host. CyaA subverts host phagocytic cells by an orchestrated action of its functional domains, where an extremely catalytically active adenylyl cyclase enzyme is delivered into phagocyte cytosol by a pore-forming repeat-in-toxin (RTX) cytolysin moiety. By targeting sentinel cells expressing the complement receptor 3, known as the CD11b/CD18 ((M2)) integrin, CyaA compromises the bactericidal functions of host phagocytes and supports infection of host airways by Bordetellae. Here, we review the state of knowledge on structural and functional aspects of CyaA toxin action, placing particular emphasis on signaling mechanisms by which the toxin-produced 3,5-cyclic adenosine monophosphate (cAMP) subverts the physiology of phagocytic cells.

  • 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)

Others

  • Publication year

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Toxins

  • ISSN

    2072-6651

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    28

  • Pages from-to

  • UT code for WoS article

    000414626100008

  • EID of the result in the Scopus database