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Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin

  1. 1. 0330518 - MBU-M 2010 RIV US eng J - Journal Article
    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
    R&D Projects: GA AV ČR IAA500200914; GA MŠk 1M0506
    Grant - others:-(XE) LSHB-CT-2003-503582 THERAVAC
    Institutional research plan: CEZ:AV0Z50200510
    Keywords : blue native electrophoresis * planar lipid bilayer membranes * pore-forming activity
    Subject RIV: EE - Microbiology, Virology
    Impact factor: 6.401, year: 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
    Permanent Link: http://hdl.handle.net/11104/0176292