Acylation of Lysine 860 Allows Tight Binding and Cytotoxicity of Bordetella Adenylate Cyclase on CD1 1b-Expressing Cells

0022198 - MBÚ 2006 RIV SIGLE US eng J - Journal Article
Mašín, Jiří - Basler, Marek - Knapp, O. - El-Azami-El-Idrissi, M. - Maier, E. - Konopásek, I. - Benz, R. - Leclerc, C. - Šebo, Peter
Acylation of Lysine 860 Allows Tight Binding and Cytotoxicity of Bordetella Adenylate Cyclase on CD1 1b-Expressing Cells.
[Acylace lysinového zbytku 860 umožňuje pevnou vazbu a cytotoxickou aktivitu adenylát-cyklazového toxinu baktérie Bordetella pertussis na buňkách exprimunjících CD11b.]
Biochemistry. Roč. 44, - (2005), s. 12766-12759. ISSN 0006-2960
R&D Projects: GA AV ČR IAA5020406; GA MŠMT 1M0506
Institutional research plan: CEZ:AV0Z50200510
Keywords : lysine 860 * bordetella
Subject RIV: EE - Microbiology, Virology
Impact factor: 3.848, year: 2005

The Bordetella adenylate cyclase toxin-hemolysin (CyaA, ACT, or AC-Hly) forms cation-selective membrane channels and delivers into the cytosol of target cells an adenylate cyclase domain (AC) that catalyzes uncontrolled conversion of cellular ATP to cAMP. Both toxin activities were previously shown to depend on post-translational activation of proCyaA to CyaA by covalent palmitoylation of the internal Lys983 residue (K983). CyaA, however, harbors a second RTX acylation site at residue Lys860 (K860), and the role of K860 acylation in toxin activity is unclear

Práce ukazuje, že jediná acylace jak na lysinu 860 tak na lysinu 983 postačuje pro těsnou interakci ACT s integrinovým receptorem CD11b/CD18. Tato funkční redundance dvou acylačních míst nemá zřejmý důvod, nicméně umožňuje průnik toxinu do buněk přes plasmatickou membránu
Permanent Link: http://hdl.handle.net/11104/0110981