Number of the records: 1

Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin

SYSNO ASEP	0330518
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin
Author(s)	Vojtová, Jana (MBU-M)_{RID, ORCID} Basler, Marek (MBU-M) Osička, Radim (MBU-M)_{RID, ORCID} Knapp, O. (DE) Maier, E. (DE) Černý, J. (CZ) Benada, Oldřich (MBU-M)_{ORCID, RID} Benz, R. (DE) Šebo, Peter (MBU-M)_{RID, ORCID}
Source Title	FASEB Journal. - : Wiley - ISSN 0892-6638 Roč. 23, - (2009), s. 2831-2843
Number of pages	13 s.
Language	eng - English
Country	US - United States
Keywords	blue native electrophoresis ; planar lipid bilayer membranes ; pore-forming activity
Subject RIV	EE - Microbiology, Virology
R&D Projects	IAA500200914 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)
UT WOS	000270241000006
DOI	10.1096/fj.09-131250
Annotation	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
Workplace	Institute of Microbiology
Contact	Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
Year of Publishing	2010

Number of the records: 1