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Differences in Purinergic Amplification of Osmotic Cell Lysis by the Pore-Forming RTX Toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the Role of Pore Size
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SYSNO ASEP 0423359 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Differences in Purinergic Amplification of Osmotic Cell Lysis by the Pore-Forming RTX Toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the Role of Pore Size Author(s) Mašín, Jiří (MBU-M) RID, ORCID
Fišer, Radovan (MBU-M) RID, ORCID
Linhartová, Irena (MBU-M) RID, ORCID
Osička, Radim (MBU-M) RID, ORCID
Bumba, Ladislav (MBU-M) RID, ORCID
Hewlett, E. L. (US)
Benz, R. (DE)
Šebo, Peter (MBU-M) RID, ORCIDSource Title Infection and Immunity. - : American Society for Microbiology - ISSN 0019-9567
Roč. 81, č. 12 (2013), s. 4571-4582Number of pages 12 s. Language eng - English Country US - United States Keywords Bordetella pertussis ; Actinobacillus pleuropneumoniae ; E-coli Subject RIV EE - Microbiology, Virology R&D Projects GAP302/12/0460 GA ČR - Czech Science Foundation (CSF) GAP302/11/0580 GA ČR - Czech Science Foundation (CSF) GAP207/11/0717 GA ČR - Czech Science Foundation (CSF) IAA500200914 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) GA13-14547S GA ČR - Czech Science Foundation (CSF) Institutional support MBU-M - RVO:61388971 UT WOS 000327066100026 DOI 10.1128/IAI.00711-13 Annotation A large subgroup of the repeat in toxin (RTX) family of leukotoxins of Gram-negative pathogens consists of pore-forming hemolysins. These can permeabilize mammalian erythrocytes (RBCs) and provoke their colloid osmotic lysis (hemolytic activity). Recently, ATP leakage through pannexin channels and P2X receptor-mediated opening of cellular calcium and potassium channels were implicated in cell permeabilization by pore-forming toxins. In the study described here, we examined the role played by purinergic signaling in the cytolytic action of two RTX toxins that form pores of different sizes. The cytolytic potency of ApxIA hemolysin of Actinobacillus pleuropneumoniae, which forms pores about 2.4 nm wide, was clearly reduced in the presence of P2X(7) receptor antagonists or an ATP scavenger, such as pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid (PPADS), Brilliant Blue G, ATP oxidized sodium salt, or hexokinase. In contrast, antagonists of purinergic signaling had no impact on the hemolytic potency of the adenylate cyclase toxin-hemolysin (CyaA) of Bordetella pertussis, which forms pores of 0.6 to 0.8 nm in diameter. Moreover, the conductance of pores formed by ApxIA increased with the toxin concentration, while the conductance of the CyaA single pore units was constant at various toxin concentrations. However, the P2X(7) receptor antagonist PPADS inhibited in a concentration-dependent manner the exacerbated hemolytic activity of a CyaA-Delta N489 construct (lacking 489 N-terminal residues of CyaA), which exhibited a strongly enhanced pore-forming propensity (>20-fold) and also formed severalfold larger conductance units in planar lipid bilayers than intact CyaA. These results point to a pore size threshold of purinergic amplification involvement in cell permeabilization by pore-forming RTX toxins Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2014
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