Calcium Influx Rescues Adenylate Cyclase-Hemolysin from Rapid Cell Membrane Removal and Enables Phagocyte Permeabilization by Toxin Pores

0377230 - MBÚ 2013 RIV US eng J - Journal Article
Fišer, Radovan - Mašín, Jiří - Bumba, Ladislav - Pospíšilová, Eva - Fayolle, C. - Basler, Marek - Sadílková, Lenka - Adkins, Irena - Kamanová, Jana - Černý, J. - Konopásek, I. - Osička, Radim - Leclerc, C. - Šebo, Peter
Calcium Influx Rescues Adenylate Cyclase-Hemolysin from Rapid Cell Membrane Removal and Enables Phagocyte Permeabilization by Toxin Pores.
PLoS Pathogens. Roč. 8, č. 4 (2012), e1002580. ISSN 1553-7366. E-ISSN 1553-7374
R&D Projects: GA ČR GA310/08/0447; GA AV ČR IAA500200914; GA ČR GP310/09/P582; GA ČR(CZ) GAP207/11/0717; GA ČR(CZ) GAP302/11/0580
Institutional research plan: CEZ:AV0Z50200510; CEZ:AV0Z50520701
Keywords : RECEPTOR-MEDIATED ENDOCYTOSIS * ANTIGEN PRESENTATION PATHWAY * COATED PIT FORMATION
Subject RIV: EE - Microbiology, Virology; EE - Microbiology, Virology (BTO-N)
Impact factor: 8.136, year: 2012

Bordetella adenylate cyclase toxin-hemolysin (CyaA) penetrates the cytoplasmic membrane of phagocytes and employs two distinct conformers to exert its multiple activities. One conformer forms cation-selective pores that permeabilize phagocyte membrane for efflux of cytosolic potassium. The other conformer conducts extracellular calcium ions across cytoplasmic membrane of cells, relocates into lipid rafts, translocates the adenylate cyclase enzyme (AC) domain into cells and converts cytosolic ATP to cAMP. We show that the calcium-conducting activity of CyaA controls the path and kinetics of endocytic removal of toxin pores from phagocyte membrane. The enzymatically inactive but calcium-conducting CyaA-AC(-) toxoid was endocytosed via a clathrin-dependent pathway
Permanent Link: http://hdl.handle.net/11104/0209449