Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin

0330518 - MBÚ 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. E-ISSN 1530-6860
R&D Projects: GA AV ČR IAA500200914; GA MŠMT 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