Počet záznamů: 1

Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin

  1. 1.
    0330518 - MBU-M 2010 RIV US eng J - Článek v odborném periodiku
    Vojtová, Jana - Basler, Marek - Osička, Radim - Knapp, O. - Maier, E. - Černý, J. - Benada, Oldřich - Benz, R. - Šebo, Peter
    Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
    FASEB Journal. Roč. 23, - (2009), s. 2831-2843 ISSN 0892-6638
    Grant CEP: GA AV ČR IAA500200914; GA MŠk 1M0506
    Grant ostatní:-(XE) LSHB-CT-2003-503582 THERAVAC
    Výzkumný záměr: CEZ:AV0Z50200510
    Klíčová slova: blue native electrophoresis * planar lipid bilayer membranes * pore-forming activity
    Kód oboru RIV: EE - Mikrobiologie, virologie
    Impakt faktor: 6.401, rok: 2009

    The Bordetella adenylate cyclase-hemolysin (CyaA, ACT, or AC-Hly) is a multifunctional toxin. CyaA delivers into host cells an adenylate cyclase enzyme (AC) and permeabilizes cell membrane by forming small cation selective pores. Indirect evidence suggested that these two activities were accomplished by different membrane-inserted CyaA conformers, one acting as an AC-delivering monomer, the other as an uncharacterized pore-forming oligomer. Here, CyaA oligomers were revealed in sheep erythrocyte membranes by immunogold labeling and directly demonstrated by pull-down of membrane-inserted CyaA together with biotinylated CyaA-AC- toxoid. Membrane oligomers of CyaA could also be resolved by non-denaturing electrophoresis of mild detergent extracts of erythrocytes
    Trvalý link: http://hdl.handle.net/11104/0176292