Number of the records: 1
Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin
- 1.
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, ORCIDSource Title FASEB Journal. - : Wiley - ISSN 0892-6638
Roč. 23, - (2009), s. 2831-2843Number 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