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

0354250 - MBÚ 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. E-ISSN 1365-2958
Grant CEP: GA AV ČR IAA500200914; GA ČR GA310/08/0447; GA MŠMT 1M0506; GA MŠMT 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