Počet záznamů: 1

Adenylate cyclase toxin translocates across target cell membrane without forming a pore

  1. 1.
    0354250 - MBU-M 2011 RIV GB eng J - Článek v odborném periodiku
    Osičková, Adriana - Mašín, Jiří - Fayolle, C. - Krůšek, Jan - Basler, Marek - Pospíšilová, Eva - Leclerc, C. - Osička, Radim - Šebo, Peter
    Adenylate cyclase toxin translocates across target cell membrane without forming a pore.
    Molecular Microbiology. Roč. 75, č. 6 (2010), s. 1550-1562 ISSN 0950-382X
    Grant CEP: GA AV ČR IAA500200914; GA ČR GA310/08/0447; GA MŠk 1M0506; GA MŠk 2B06161
    Výzkumný záměr: CEZ:AV0Z50110509; CEZ:AV0Z50200510
    Klíčová slova: ANTIGEN PRESENTATION PATHWAY * BORDETELLA-PERTUSSIS * INVASIVE ACTIVITY
    Kód oboru RIV: EE - Mikrobiologie, virologie
    Impakt faktor: 4.819, rok: 2010

    The adenylate cyclase toxin-haemolysin of Bordetella (CyaA) targets CD11b plus myeloid phagocytes and translocates across their cytoplasmic membrane an adenylate cyclase (AC) enzyme that catalyses conversion of cytosolic ATP into cAMP. In parallel, CyaA acts as a cytolysin forming cation-selective pores, which permeabilize cell membrane and eventually provoke cell lysis. Using cytolytic activity, potassium efflux and patch-clamp assays, we show that a combination of substitutions within the pore-forming (E570Q) and acylation-bearing domain (K860R) ablates selectively the cell-permeabilizing activity of CyaA. At the same time, however, the capacity of such mutant CyaA to translocate the AC domain across cytoplasmic membrane into cytosol of macrophage cells and to elevate cellular cAMP concentrations remained intact
    Trvalý link: http://hdl.handle.net/11104/0193297