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

SYSNO ASEP	0022198
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Ostatní články
Title	Acylation of Lysine 860 Allows Tight Binding and Cytotoxicity of Bordetella Adenylate Cyclase on CD1 1b-Expressing Cells
Title	Acylace lysinového zbytku 860 umožňuje pevnou vazbu a cytotoxickou aktivitu adenylát-cyklazového toxinu baktérie Bordetella pertussis na buňkách exprimunjících CD11b
Author(s)	Mašín, Jiří (MBU-M)_{RID, ORCID} Basler, Marek (MBU-M) Knapp, O. (DE) El-Azami-El-Idrissi, M. (FR) Maier, E. (DE) Konopásek, I. (CZ) Benz, R. (DE) Leclerc, C. (FR) Šebo, Peter (MBU-M)_{RID, ORCID}
Source Title	Biochemistry. - : American Chemical Society - ISSN 0006-2960 Roč. 44, - (2005), s. 12766-12759
Number of pages	7 s.
Language	eng - English
Country	US - United States
Keywords	lysine 860 ; bordetella
Subject RIV	EE - Microbiology, Virology
R&D Projects	IAA5020406 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
	1M0506 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
CEZ	AV0Z50200510 - MBU-M (2005-2011)
Annotation	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
Workplace	Institute of Microbiology
Contact	Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
Year of Publishing	2006

Number of the records: 1