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Transmembrane segments of complement receptor 3 do not participate in cytotoxic activities but determine receptor structure required for action of Bordetella adenylate cyclase toxin

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081715%3A_____%2F16%3A00460039" target="_blank" >RIV/68081715:_____/16:00460039 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/16:00460039 RIV/00216208:11310/16:10331578

  • Result on the web

    <a href="http://dx.doi.org/10.1093/femspd/ftw008" target="_blank" >http://dx.doi.org/10.1093/femspd/ftw008</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/femspd/ftw008" target="_blank" >10.1093/femspd/ftw008</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Transmembrane segments of complement receptor 3 do not participate in cytotoxic activities but determine receptor structure required for action of Bordetella adenylate cyclase toxin

  • Original language description

    Adenylate cyclase toxin-hemolysin (CyaA, ACT or AC-Hly) of the whooping cough agent Bordetella pertussis penetrates phagocytes expressing the integrin complement receptor 3 (CR3, CD11b/CD18, alpha(M)beta(2) or Mac-1). CyaA translocates its adenylate cyclase (AC) enzyme domain into cell cytosol and catalyzes unregulated conversion of ATP to cAMP, thereby subverting cellular signaling. In parallel, CyaA forms small cation-selective membrane pores that permeabilize cells for potassium efflux, contributing to cytotoxicity of CyaA and eventually provoking colloid-osmotic cell lysis. To investigate whether the single-pass alpha-helical transmembrane segments of CR3 subunits CD11b and CD18 do directly participate in AC domain translocation and/or pore formation by the toxin, we expressed in CHO cells variants of CR3 that contained artificial transmembrane segments, or lacked the transmembrane segment(s) at all. The results demonstrate that the transmembrane segments of CR3 are not directly involved in the cytotoxic activities of CyaA but serve for maintaining CR3 in a conformation that is required for efficient toxin binding and action.

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    CB - Analytical chemistry, separation

  • OECD FORD branch

Result continuities

  • Project

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

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • 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

    74

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    13

  • Pages from-to

  • UT code for WoS article

    000374475700012

  • EID of the result in the Scopus database